Target Binding Site Detail

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Target General Information
Ligand General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T48598 Target Info
Target Name GTPase KRas (KRAS)
Synonyms c-Ki-ras; c-K-ras; RASK2; Ki-Ras; KRAS2; K-Ras 2
Target Type Clinical trial Target
Gene Name KRAS
Biochemical Class Small GTPase
UniProt ID
RASK_HUMAN
Ligand General Information  Top
Ligand Name Phosphoaminophosphonic acid-guanylate ester Ligand Info
Canonical SMILES C1=NC2=C(N1C3C(C(C(O3)COP(=O)(O)OP(=O)(NP(=O)(O)O)O)O)O)N=C(NC2=O)N
InChI 1S/C10H17N6O13P3/c11-10-13-7-4(8(19)14-10)12-2-16(7)9-6(18)5(17)3(28-9)1-27-32(25,26)29-31(23,24)15-30(20,21)22/h2-3,5-6,9,17-18H,1H2,(H,25,26)(H3,11,13,14,19)(H4,15,20,21,22,23,24)/t3-,5-,6-,9-/m1/s1
InChIKey UQABYHGXWYXDTK-UUOKFMHZSA-N
PubChem Compound ID 135403657
Drug Binding Sites of Target  Top
PDB ID: 5OCG      Discovery of small molecules binding to KRAS via high affinity antibody fragment competition method.
Method X-ray diffraction Resolution 1.48 Å Mutation Yes [1]
PDB Sequence
STEYKLVVVG
10
ADGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHHYREQI
100

KRVKDSEDVP
110
MVLVGNKCDL
120
PSRTVDTKQA
130
QDLARSYGIP
140
FIETSAKTRQ
150

GVDDAFYTLV
160
REIRKHKEKM
170
SK
Residue
Distance (Å)
GLY10
4.899
ALA11
3.839
ASP12
3.404
GLY13
3.257
VAL14
3.121
GLY15
3.000
LYS16
2.671
SER17
2.858
ALA18
2.767
LEU19
4.987
PHE28
3.340
VAL29
2.594
ASP30
2.952
GLU31
3.449
TYR32
3.520
ASP33
4.312
Residue
Distance (Å)
PRO34
3.276
THR35
2.949
ASP57
4.743
THR58
4.090
ALA59
4.053
GLY60
3.031
ASN116
3.202
LYS117
3.121
CYS118
4.817
ASP119
2.763
LEU120
3.478
THR144
4.669
SER145
3.468
ALA146
2.921
LYS147
3.588
PDB ID: 5USJ      Crystal Structure of human KRAS G12D mutant in complex with GDPNP
Method X-ray diffraction Resolution 1.94 Å Mutation Yes [2]
PDB Sequence
GSHMTEYKLV
7
VVGADGVGKS
17
ALTIQLIQNH
27
FVDEYDPTIE
37
DSYRKQVVID
47

GETCLLDILD
57
TAGYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHHYREQI
100

KRVKDSEDVP
110
MVLVGNKCDL
120
PSRTVDTKQA
130
QDLARSYGIP
140
FIETSAKTRQ
150

GVDDAFYTLV
160
REIRKHKE
Residue
Distance (Å)
GLY10
4.707
ALA11
3.897
ASP12
3.308
GLY13
3.038
VAL14
3.271
GLY15
3.047
LYS16
2.495
SER17
2.892
ALA18
2.761
LEU19
4.996
PHE28
3.310
VAL29
2.692
ASP30
2.833
GLU31
3.882
TYR32
3.145
ASP33
4.291
Residue
Distance (Å)
PRO34
3.381
THR35
3.051
ASP57
4.537
THR58
4.124
ALA59
4.000
GLY60
2.962
ASN116
3.097
LYS117
3.263
CYS118
4.790
ASP119
2.723
LEU120
3.612
THR144
4.719
SER145
3.375
ALA146
2.788
LYS147
3.603
PDB ID: 7VVB      Crystal Structure of KRas4A(GMPPNP-bound) in complex with the Ras-binding domain(RBD) of SIN1
Method X-ray diffraction Resolution 1.70 Å Mutation No [3]
PDB Sequence
GMTEYKLVVV
9
GAGGVGKSAL
19
TIQLIQNHFV
29
DEYDPTIEDS
39
YRKQVVIDGE
49

TCLLDILDTA
59
GQEEYSAMRD
69
QYMRTGEGFL
79
CVFAINNTKS
89
FEDIHHYREQ
99

IKRVKDSEDV
109
PMVLVGNKCD
119
LPSRTVDTKQ
129
AQDLARSYGI
139
PFIETSAKTR
149

QRVEDAFYTL
159
VREIRQY
Residue
Distance (Å)
GLY10
4.718
ALA11
3.942
GLY12
3.521
GLY13
3.080
VAL14
3.322
GLY15
3.073
LYS16
2.596
SER17
2.925
ALA18
2.822
PHE28
3.334
VAL29
2.691
ASP30
2.797
GLU31
3.546
TYR32
3.639
ASP33
4.378
PRO34
3.362
Residue
Distance (Å)
THR35
2.926
ASP57
4.606
THR58
4.100
ALA59
3.959
GLY60
2.829
GLN61
4.340
ASN116
3.172
LYS117
3.291
CYS118
4.925
ASP119
2.869
LEU120
3.626
THR144
4.815
SER145
3.577
ALA146
2.865
LYS147
3.566
PDB ID: 6CC9      NMR data-driven model of GTPase KRas-GMPPNP:Cmpd2 complex tethered to a nanodisc
Method Solution NMR Resolution N.A. Mutation Yes [4]
PDB Sequence
MTEYKLVVVG
10
AVGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHHYREQI
100

KRVKDSEDVP
110
MVLVGNKCDL
120
PSRTVDTKQA
130
QDLARSYGIP
140
FIETSAKTRQ
150

GVDDAFYTLV
160
REIRKHKEKM
170
SKDGKKKKKK
180
SKTKC
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .B:11 or .B:12 or .B:13 or .B:14 or .B:15 or .B:16 or .B:17 or .B:18 or .B:28 or .B:29 or .B:30 or .B:31 or .B:32 or .B:33 or .B:34 or .B:35 or .B:116 or .B:117 or .B:118 or .B:119 or .B:120 or .B:145 or .B:146 or .B:147 or .B:148; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ALA11
4.719
VAL12
3.345
GLY13
2.192
VAL14
3.496
GLY15
2.310
LYS16
2.605
SER17
2.090
ALA18
3.448
PHE28
3.351
VAL29
3.403
ASP30
3.058
GLU31
2.841
TYR32
3.469
Residue
Distance (Å)
ASP33
2.885
PRO34
3.223
THR35
4.076
ASN116
2.888
LYS117
2.867
CYS118
4.096
ASP119
2.864
LEU120
3.319
SER145
1.974
ALA146
2.560
LYS147
2.557
THR148
4.728
PDB ID: 6CCH      NMR data-driven model of GTPase KRas-GMPPNP tethered to a nanodisc (E3 state)
Method Solution NMR Resolution N.A. Mutation Yes [4]
PDB Sequence
MTEYKLVVVG
10
AVGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHHYREQI
100

KRVKDSEDVP
110
MVLVGNKCDL
120
PSRTVDTKQA
130
QDLARSYGIP
140
FIETSAKTRQ
150

GVDDAFYTLV
160
REIRKHKEKM
170
SKDGKKKKKK
180
SKTKC
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .B:11 or .B:12 or .B:13 or .B:14 or .B:15 or .B:16 or .B:17 or .B:18 or .B:28 or .B:29 or .B:30 or .B:31 or .B:32 or .B:33 or .B:34 or .B:35 or .B:57 or .B:58 or .B:60 or .B:116 or .B:117 or .B:119 or .B:120 or .B:145 or .B:146 or .B:147; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ALA11
4.718
VAL12
3.443
GLY13
1.942
VAL14
2.668
GLY15
3.665
LYS16
3.010
SER17
2.016
ALA18
3.548
PHE28
3.361
VAL29
3.483
ASP30
2.832
GLU31
3.655
TYR32
3.312
Residue
Distance (Å)
ASP33
2.741
PRO34
2.945
THR35
2.681
ASP57
4.313
THR58
4.248
GLY60
3.845
ASN116
2.845
LYS117
3.293
ASP119
3.000
LEU120
3.517
SER145
3.803
ALA146
2.051
LYS147
3.114
PDB ID: 6CCX      NMR data-driven model of GTPase KRas-GMPPNP:Cmpd2 complex tethered to a nanodisc
Method Solution NMR Resolution N.A. Mutation Yes [4]
PDB Sequence
MTEYKLVVVG
10
AVGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHHYREQI
100

KRVKDSEDVP
110
MVLVGNKCDL
120
PSRTVDTKQA
130
QDLARSYGIP
140
FIETSAKTRQ
150

GVDDAFYTLV
160
REIRKHKEKM
170
SKDGKKKKKK
180
SKTKC
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .B:11 or .B:12 or .B:13 or .B:14 or .B:15 or .B:16 or .B:17 or .B:18 or .B:19 or .B:28 or .B:29 or .B:30 or .B:31 or .B:32 or .B:33 or .B:34 or .B:35 or .B:57 or .B:60 or .B:116 or .B:117 or .B:119 or .B:120 or .B:145 or .B:146 or .B:147; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ALA11
3.743
VAL12
3.512
GLY13
2.061
VAL14
3.315
GLY15
2.867
LYS16
2.246
SER17
2.036
ALA18
2.482
LEU19
4.864
PHE28
3.537
VAL29
3.540
ASP30
2.847
GLU31
3.955
Residue
Distance (Å)
TYR32
3.068
ASP33
2.786
PRO34
3.262
THR35
2.671
ASP57
4.321
GLY60
4.794
ASN116
2.775
LYS117
3.246
ASP119
3.081
LEU120
3.979
SER145
3.932
ALA146
2.099
LYS147
3.110
PDB ID: 5OCO      Discovery of small molecules binding to KRAS via high affinity antibody fragment competition method.
Method X-ray diffraction Resolution 1.66 Å Mutation Yes [1]
PDB Sequence
YFQGMTEYKL
6
VVVGAGGVGK
16
SALTIQLIQN
26
HFVDEYDPTI
36
EDSYRKQVVI
46

DGETLLDILD
57
TAGHEEYSAM
67
RDQYMRTGEG
77
FLCVFAINNT
87
KSFEDIHHYR
97

EQIKRVKDSE
107
DVPMVLVGNK
117
CDLPSRTVDT
127
KQAQDLARSY
137
GIPFIETSAK
147

TRQGVDDAFY
157
TLVREIRKHK
167
EK
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .B:10 or .B:11 or .B:12 or .B:13 or .B:14 or .B:15 or .B:16 or .B:17 or .B:18 or .B:28 or .B:29 or .B:30 or .B:31 or .B:32 or .B:33 or .B:34 or .B:35 or .B:57 or .B:58 or .B:59 or .B:60 or .B:116 or .B:117 or .B:118 or .B:119 or .B:120 or .B:144 or .B:145 or .B:146 or .B:147; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY10
4.832
ALA11
3.859
GLY12
3.451
GLY13
3.061
VAL14
3.250
GLY15
3.053
LYS16
2.684
SER17
2.988
ALA18
2.755
PHE28
3.369
VAL29
2.630
ASP30
2.861
GLU31
3.475
TYR32
3.647
ASP33
4.346
Residue
Distance (Å)
PRO34
3.305
THR35
2.915
ASP57
4.749
THR58
4.117
ALA59
3.939
GLY60
2.896
ASN116
3.071
LYS117
3.200
CYS118
4.812
ASP119
2.781
LEU120
3.491
THR144
4.623
SER145
3.464
ALA146
2.845
LYS147
3.819
PDB ID: 5OCT      Discovery of small molecules binding to KRAS via high affinity antibody fragment competition method.
Method X-ray diffraction Resolution 2.07 Å Mutation Yes [1]
PDB Sequence
YFQGMTEYKL
6
VVVGAGGVGK
16
SALTIQLIQN
26
HFVDEYDPTI
36
EDSYRKQVVI
46

DGETLLDILD
57
TAGHEEYSAM
67
RDQYMRTGEG
77
FLCVFAINNT
87
KSFEDIHHYR
97

EQIKRVKDSE
107
DVPMVLVGNK
117
CDLPSRTVDT
127
KQAQDLARSY
137
GIPFIETSAK
147

TRQGVDDAFY
157
TLVREIRKHK
167
E
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:10 or .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY10
4.758
ALA11
3.831
GLY12
3.493
GLY13
3.082
VAL14
3.412
GLY15
3.190
LYS16
2.578
SER17
2.938
ALA18
2.737
PHE28
3.451
VAL29
2.634
ASP30
2.813
GLU31
3.508
TYR32
3.588
ASP33
4.340
Residue
Distance (Å)
PRO34
3.397
THR35
2.795
ASP57
4.695
THR58
4.141
ALA59
3.803
GLY60
2.933
ASN116
3.051
LYS117
3.204
CYS118
4.774
ASP119
2.838
LEU120
3.571
THR144
4.582
SER145
3.313
ALA146
2.817
LYS147
3.685
PDB ID: 3GFT      Human K-Ras (Q61H) in complex with a GTP analogue
Method X-ray diffraction Resolution 2.27 Å Mutation No [5]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
HEEYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHHYREQI
100

KRVKDSEDVP
110
MVLVGNKCDL
120
PSRTVDTKQA
130
QDLARSYGIP
140
FIETSAKTRQ
150

GVDDAFYTLV
160
REIRKHK
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:10 or .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:61 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY10
4.671
ALA11
3.860
GLY12
3.641
GLY13
3.163
VAL14
3.329
GLY15
3.215
LYS16
2.701
SER17
2.944
ALA18
2.816
PHE28
3.385
VAL29
2.504
ASP30
2.771
GLU31
3.535
TYR32
2.604
ASP33
4.295
PRO34
3.630
Residue
Distance (Å)
THR35
2.838
ASP57
4.693
THR58
3.933
ALA59
3.831
GLY60
2.764
HIS61
4.409
ASN116
3.126
LYS117
3.305
CYS118
4.738
ASP119
2.621
LEU120
3.566
THR144
4.681
SER145
3.391
ALA146
2.793
LYS147
3.691
PDB ID: 6PTS      NMR data-driven model of KRas-GMPPNP:RBD-CRD complex tethered to a nanodisc (state A)
Method Solution NMR Resolution N.A. Mutation No [6]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHHYREQI
100

KRVKDSEDVP
110
MVLVGNKCDL
120
PSRTVDTKQA
130
QDLARSYGIP
140
FIETSAKTRQ
150

GVDDAFYTLV
160
REIRKHKEKM
170
SKDGKKKKKK
180
SKTKC
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .B:12 or .B:13 or .B:14 or .B:15 or .B:16 or .B:17 or .B:18 or .B:19 or .B:28 or .B:29 or .B:30 or .B:31 or .B:32 or .B:33 or .B:34 or .B:35 or .B:57 or .B:58 or .B:59 or .B:60 or .B:116 or .B:117 or .B:119 or .B:120 or .B:145 or .B:146 or .B:147 or .B:148; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY12
4.110
GLY13
2.305
VAL14
3.829
GLY15
2.371
LYS16
1.691
SER17
1.802
ALA18
1.850
LEU19
4.385
PHE28
3.969
VAL29
3.257
ASP30
4.190
GLU31
4.411
TYR32
3.091
ASP33
3.067
Residue
Distance (Å)
PRO34
3.683
THR35
1.584
ASP57
4.474
THR58
3.593
ALA59
4.867
GLY60
3.244
ASN116
1.863
LYS117
2.808
ASP119
3.212
LEU120
2.959
SER145
3.273
ALA146
1.846
LYS147
1.792
THR148
4.125
PDB ID: 6PTW      NMR data-driven model of KRas-GMPPNP:RBD-CRD complex tethered to a nanodisc (state B)
Method Solution NMR Resolution N.A. Mutation No [6]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHHYREQI
100

KRVKDSEDVP
110
MVLVGNKCDL
120
PSRTVDTKQA
130
QDLARSYGIP
140
FIETSAKTRQ
150

GVDDAFYTLV
160
REIRKHKEKM
170
SKDGKKKKKK
180
SKTKC
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .B:11 or .B:12 or .B:13 or .B:14 or .B:15 or .B:16 or .B:17 or .B:18 or .B:19 or .B:28 or .B:29 or .B:30 or .B:31 or .B:32 or .B:33 or .B:34 or .B:35 or .B:57 or .B:58 or .B:59 or .B:60 or .B:61 or .B:116 or .B:117 or .B:118 or .B:119 or .B:120 or .B:144 or .B:145 or .B:146 or .B:147 or .B:148; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ALA11
3.387
GLY12
3.852
GLY13
1.853
VAL14
2.015
GLY15
2.190
LYS16
1.702
SER17
1.758
ALA18
1.773
LEU19
4.305
PHE28
3.836
VAL29
2.821
ASP30
2.171
GLU31
4.084
TYR32
1.796
ASP33
3.481
PRO34
3.456
Residue
Distance (Å)
THR35
2.162
ASP57
4.281
THR58
4.084
ALA59
4.763
GLY60
2.917
GLN61
4.135
ASN116
1.916
LYS117
2.467
CYS118
4.753
ASP119
3.439
LEU120
2.912
THR144
4.786
SER145
2.633
ALA146
1.766
LYS147
2.815
THR148
4.359
PDB ID: 6FA1      Antibody derived (Abd-4) small molecule binding to KRAS.
Method X-ray diffraction Resolution 1.97 Å Mutation Yes [1]
PDB Sequence
> Chain A
AFQGMTEYKL
6
VVVGAGGVGK
16
SALTIQLIQN
26
HFVDEYDPTI
36
EDSYRKQVVI
46

DGETLLDILD
57
TAGHEEYSAM
67
RDQYMRTGEG
77
FLCVFAINNT
87
KSFEDIHHYR
97

EQIKRVKDSE
107
DVPMVLVGNK
117
CDLPSRTVDT
127
KQAQDLARSY
137
GIPFIETSAK
147

TRQGVDDAFY
157
TLVREIRKHK
167
E
> Chain B
AFQGMTEYKL
6
VVVGAGGVGK
16
SALTIQLIQN
26
HFVDEYDPTI
36
EDSYRKQVVI
46

DGETLLDILD
57
TAGHEEYSAM
67
RDQYMRTGEG
77
FLCVFAINNT
87
KSFEDIHHYR
97

EQIKRVKDSE
107
DVPMVLVGNK
117
CDLPSRTVDT
127
KQAQDLARSY
137
GIPFIETSAK
147

TRQGVDDAFY
157
TLVREIRKHK
167
EK
> Chain E
AFQGMTEYKL
6
VVVGAGGVGK
16
SALTIQLIQN
26
HFVDEYDPTI
36
EDSYRKQVVI
46

DGETCLLDIL
56
DTAGHEEYSA
66
MRDQYMRTGE
76
GFLCVFAINN
86
TKSFEDIHHY
96

REQIKRVKDS
106
EDVPMVLVGN
116
KCDLPSRTVD
126
TKQAQDLARS
136
YGIPFIETSA
146

KTRQGVDDAF
156
YTLVREIRKH
166
KEK
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:10 or .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147 or .B:10 or .B:11 or .B:12 or .B:13 or .B:14 or .B:15 or .B:16 or .B:17 or .B:18 or .B:28 or .B:29 or .B:30 or .B:31 or .B:32 or .B:33 or .B:34 or .B:35 or .B:57 or .B:58 or .B:59 or .B:60 or .B:116 or .B:117 or .B:118 or .B:119 or .B:120 or .B:144 or .B:145 or .B:146 or .B:147 or .E:10 or .E:11 or .E:12 or .E:13 or .E:14 or .E:15 or .E:16 or .E:17 or .E:18 or .E:28 or .E:29 or .E:30 or .E:31 or .E:32 or .E:33 or .E:34 or .E:35 or .E:57 or .E:58 or .E:59 or .E:60 or .E:116 or .E:117 or .E:118 or .E:119 or .E:120 or .E:144 or .E:145 or .E:146 or .E:147; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue [Chain]
Distance (Å)
GLY10[A]
4.846
ALA11[A]
3.914
GLY12[A]
3.482
GLY13[A]
2.986
VAL14[A]
3.291
GLY15[A]
3.047
LYS16[A]
2.633
SER17[A]
2.963
ALA18[A]
2.772
PHE28[A]
3.402
VAL29[A]
2.614
ASP30[A]
2.862
GLU31[A]
3.541
TYR32[A]
3.595
ASP33[A]
4.319
PRO34[A]
3.424
THR35[A]
2.777
ASP57[A]
4.738
THR58[A]
4.161
ALA59[A]
3.930
GLY60[A]
2.979
ASN116[A]
2.992
LYS117[A]
3.274
CYS118[A]
4.765
ASP119[A]
2.875
LEU120[A]
3.613
THR144[A]
4.556
SER145[A]
3.348
ALA146[A]
2.846
LYS147[A]
3.742
GLY10[B]
4.813
ALA11[B]
3.827
GLY12[B]
3.505
GLY13[B]
3.087
VAL14[B]
3.275
GLY15[B]
3.080
LYS16[B]
2.569
SER17[B]
2.942
ALA18[B]
2.782
PHE28[B]
3.375
VAL29[B]
2.638
ASP30[B]
2.869
GLU31[B]
3.588
TYR32[B]
3.653
ASP33[B]
4.299
Residue [Chain]
Distance (Å)
PRO34[B]
3.270
THR35[B]
2.811
ASP57[B]
4.741
THR58[B]
4.037
ALA59[B]
3.957
GLY60[B]
2.925
ASN116[B]
3.054
LYS117[B]
3.316
CYS118[B]
4.878
ASP119[B]
2.879
LEU120[B]
3.634
THR144[B]
4.608
SER145[B]
3.392
ALA146[B]
2.782
LYS147[B]
3.707
GLY10[E]
4.925
ALA11[E]
3.830
GLY12[E]
3.682
GLY13[E]
3.009
VAL14[E]
3.376
GLY15[E]
3.124
LYS16[E]
2.688
SER17[E]
3.049
ALA18[E]
2.762
PHE28[E]
3.388
VAL29[E]
2.704
ASP30[E]
2.986
GLU31[E]
3.660
TYR32[E]
3.410
ASP33[E]
4.338
PRO34[E]
3.493
THR35[E]
2.973
ASP57[E]
4.762
THR58[E]
4.162
ALA59[E]
3.809
GLY60[E]
2.755
ASN116[E]
3.058
LYS117[E]
3.136
CYS118[E]
4.932
ASP119[E]
2.884
LEU120[E]
3.735
THR144[E]
4.596
SER145[E]
3.386
ALA146[E]
2.795
LYS147[E]
3.741
PDB ID: 6FA4      Antibody derived (Abd-7) small molecule binding to KRAS.
Method X-ray diffraction Resolution 2.02 Å Mutation Yes [1]
PDB Sequence
> Chain A
AFQGMTEYKL
6
VVVGAGGVGK
16
SALTIQLIQN
26
HFVDEYDPTI
36
EDSYRKQVVI
46

DGETCLLDIL
56
DTAGHEEYSA
66
MRDQYMRTGE
76
GFLCVFAINN
86
TKSFEDIHHY
96

REQIKRVKDS
106
EDVPMVLVGN
116
KCDLPSRTVD
126
TKQAQDLARS
136
YGIPFIETSA
146

KTRQGVDDAF
156
YTLVREIRKH
166
KE
> Chain B
AFQGMTEYKL
6
VVVGAGGVGK
16
SALTIQLIQN
26
HFVDEYDPTI
36
EDSYRKQVVI
46

DGETLLDILD
57
TAGHEEYSAM
67
RDQYMRTGEG
77
FLCVFAINNT
87
KSFEDIHHYR
97

EQIKRVKDSE
107
DVPMVLVGNK
117
CDLPSRTVDT
127
KQAQDLARSY
137
GIPFIETSAK
147

TRQGVDDAFY
157
TLVREIRKHK
167
EK
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:10 or .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147 or .B:10 or .B:11 or .B:12 or .B:13 or .B:14 or .B:15 or .B:16 or .B:17 or .B:18 or .B:28 or .B:29 or .B:30 or .B:31 or .B:32 or .B:33 or .B:34 or .B:35 or .B:57 or .B:58 or .B:59 or .B:60 or .B:116 or .B:117 or .B:118 or .B:119 or .B:120 or .B:144 or .B:145 or .B:146 or .B:147; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue [Chain]
Distance (Å)
GLY10[A]
4.945
ALA11[A]
3.806
GLY12[A]
3.621
GLY13[A]
3.122
VAL14[A]
3.383
GLY15[A]
3.186
LYS16[A]
2.676
SER17[A]
2.991
ALA18[A]
2.676
LEU19[A]
4.962
PHE28[A]
3.309
VAL29[A]
2.601
ASP30[A]
3.003
GLU31[A]
3.533
TYR32[A]
3.710
ASP33[A]
4.478
PRO34[A]
3.363
THR35[A]
2.789
ASP57[A]
4.774
THR58[A]
4.118
ALA59[A]
3.988
GLY60[A]
2.916
ASN116[A]
3.084
LYS117[A]
3.247
CYS118[A]
4.837
ASP119[A]
2.840
LEU120[A]
3.576
THR144[A]
4.745
SER145[A]
3.449
ALA146[A]
2.854
LYS147[A]
3.611
Residue [Chain]
Distance (Å)
GLY10[B]
4.991
ALA11[B]
3.947
GLY12[B]
3.559
GLY13[B]
3.074
VAL14[B]
3.275
GLY15[B]
2.987
LYS16[B]
2.675
SER17[B]
3.029
ALA18[B]
2.754
PHE28[B]
3.362
VAL29[B]
2.669
ASP30[B]
2.808
GLU31[B]
3.599
TYR32[B]
3.652
ASP33[B]
4.291
PRO34[B]
3.251
THR35[B]
2.895
ASP57[B]
4.665
THR58[B]
4.160
ALA59[B]
4.050
GLY60[B]
2.974
ASN116[B]
3.091
LYS117[B]
3.118
CYS118[B]
4.933
ASP119[B]
2.743
LEU120[B]
3.436
THR144[B]
4.727
SER145[B]
3.465
ALA146[B]
2.822
LYS147[B]
3.661
PDB ID: 6GOG      KRAS-169 Q61H GPPNHP
Method X-ray diffraction Resolution 2.05 Å Mutation Yes [7]
PDB Sequence
FQGMTEYKLV
7
VVGAGGVGKS
17
ALTIQLIQNH
27
FVDEYDPTIE
37
DSYRKQVVID
47

GETCLLDILD
57
TAGHEEYSAM
67
RDQYMRTGEG
77
FLCVFAINNT
87
KSFEDIHHYR
97

EQIKRVKDSE
107
DVPMVLVGNK
117
CDLPSRTVDT
127
KQAQDLARSY
137
GIPFIETSAK
147

TRQGVDDAFY
157
TLVREIRKHK
167
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:10 or .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:61 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY10
4.841
ALA11
3.854
GLY12
3.658
GLY13
3.041
VAL14
3.205
GLY15
3.002
LYS16
2.656
SER17
2.943
ALA18
2.749
PHE28
3.307
VAL29
2.609
ASP30
2.809
GLU31
3.582
TYR32
3.684
ASP33
4.263
PRO34
3.408
Residue
Distance (Å)
THR35
2.843
ASP57
4.703
THR58
4.077
ALA59
3.959
GLY60
2.878
HIS61
4.722
ASN116
3.172
LYS117
3.268
CYS118
4.799
ASP119
2.775
LEU120
3.537
THR144
4.695
SER145
3.423
ALA146
2.813
LYS147
3.622
PDB ID: 6F76      Antibody derived (Abd-8) small molecule binding to KRAS.
Method X-ray diffraction Resolution 2.20 Å Mutation Yes [8]
PDB Sequence
AFQGMTEYKL
6
VVVGAGGVGK
16
SALTIQLIQN
26
HFVDEYDPTI
36
EDSYRKQVVI
46

DGETCLLDIL
56
DTAGHEEYSA
66
MRDQYMRTGE
76
GFLCVFAINN
86
TKSFEDIHHY
96

REQIKRVKDS
106
EDVPMVLVGN
116
KCDLPSRTVD
126
TKQAQDLARS
136
YGIPFIETSA
146

KTRQGVDDAF
156
YTLVREIRKH
166
KE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .B:10 or .B:11 or .B:12 or .B:13 or .B:14 or .B:15 or .B:16 or .B:17 or .B:18 or .B:28 or .B:29 or .B:30 or .B:31 or .B:32 or .B:33 or .B:34 or .B:35 or .B:57 or .B:58 or .B:59 or .B:60 or .B:116 or .B:117 or .B:118 or .B:119 or .B:120 or .B:144 or .B:145 or .B:146 or .B:147; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY10
4.957
ALA11
3.938
GLY12
3.726
GLY13
3.161
VAL14
3.360
GLY15
3.040
LYS16
2.575
SER17
3.098
ALA18
2.808
PHE28
3.395
VAL29
2.593
ASP30
2.764
GLU31
3.638
TYR32
3.714
ASP33
4.371
Residue
Distance (Å)
PRO34
3.494
THR35
2.857
ASP57
4.764
THR58
4.092
ALA59
3.976
GLY60
2.999
ASN116
3.043
LYS117
3.197
CYS118
4.944
ASP119
2.708
LEU120
3.487
THR144
4.743
SER145
3.441
ALA146
2.827
LYS147
3.655
PDB ID: 6GOE      KRAS full length G12V GPPNHP
Method X-ray diffraction Resolution 1.60 Å Mutation Yes [7]
PDB Sequence
GSTEYKLVVV
9
GAVGVGKSAL
19
TIQLIQNHFV
29
DEYDPTIEDS
39
YRKQVVIDGE
49

TCLLDILDTA
59
GQMRDQYMRT
74
GEGFLCVFAI
84
NNTKSFEDIH
94
HYREQIKRVK
104

DSEDVPMVLV
114
GNKCDLPSRT
124
VDTKQAQDLA
134
RSYGIPFIET
144
SAKTRQGVDD
154

AFYTLVREIR
164
KHKEKMS
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:10 or .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:61 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY10
4.910
ALA11
3.952
VAL12
3.582
GLY13
3.191
VAL14
3.327
GLY15
3.067
LYS16
2.612
SER17
2.947
ALA18
2.821
PHE28
3.401
VAL29
2.890
ASP30
2.742
GLU31
4.351
TYR32
2.409
ASP33
4.474
PRO34
3.599
Residue
Distance (Å)
THR35
2.972
ASP57
4.750
THR58
4.282
ALA59
4.055
GLY60
2.965
GLN61
4.942
ASN116
3.235
LYS117
3.274
CYS118
4.938
ASP119
2.832
LEU120
3.497
THR144
4.820
SER145
3.564
ALA146
2.934
LYS147
3.500
PDB ID: 6GOM      KRAS-169 Q61H GPPNHP + PPIN-1
Method X-ray diffraction Resolution 1.63 Å Mutation Yes [7]
PDB Sequence
FQGMTEYKLV
7
VVGAGGVGKS
17
ALTIQLIQNH
27
FVDEYDPTIE
37
DSYRKQVVID
47

GETLLDILDT
58
AGHEEYSAMR
68
DQYMRTGEGF
78
LCVFAINNTK
88
SFEDIHHYRE
98

QIKRVKDSED
108
VPMVLVGNKC
118
DLPSRTVDTK
128
QAQDLARSYG
138
IPFIETSAKT
148

RQGVDDAFYT
158
LVREIRKHKE
168
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:10 or .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:61 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY10
4.913
ALA11
3.925
GLY12
3.600
GLY13
3.091
VAL14
3.253
GLY15
3.083
LYS16
2.723
SER17
2.968
ALA18
2.827
PHE28
3.385
VAL29
2.713
ASP30
2.905
GLU31
3.499
TYR32
3.762
ASP33
4.380
PRO34
3.493
Residue
Distance (Å)
THR35
2.891
ASP57
4.831
THR58
4.123
ALA59
3.988
GLY60
2.942
HIS61
4.557
ASN116
3.163
LYS117
3.351
CYS118
4.876
ASP119
2.863
LEU120
3.504
THR144
4.738
SER145
3.485
ALA146
2.877
LYS147
3.710
PDB ID: 6GOD      KRAS full length wild-type GPPNHP
Method X-ray diffraction Resolution 1.71 Å Mutation No [7]
PDB Sequence
STEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHHYREQI
100

KRVKDSEDVP
110
MVLVGNKCDL
120
PSRTVDTKQA
130
QDLARSYGIP
140
FIETSAKTRQ
150

GVDDAFYTLV
160
REIRKHKEKM
170
SK
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:10 or .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:116 or .A:117 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY10
4.934
ALA11
3.885
GLY12
3.512
GLY13
3.106
VAL14
3.207
GLY15
3.070
LYS16
2.608
SER17
2.898
ALA18
2.759
PHE28
3.268
VAL29
2.837
ASP30
2.867
GLU31
3.544
TYR32
3.543
ASP33
4.361
Residue
Distance (Å)
PRO34
3.480
THR35
2.862
ASP57
4.611
THR58
4.173
ALA59
3.795
GLY60
2.879
ASN116
3.182
LYS117
3.181
ASP119
2.817
LEU120
3.815
THR144
4.689
SER145
3.417
ALA146
2.901
LYS147
3.562
PDB ID: 6FA3      Antibody derived (Abd-6) small molecule binding to KRAS.
Method X-ray diffraction Resolution 1.82 Å Mutation Yes [1]
PDB Sequence
> Chain A
FQGMTEYKLV
7
VVGAGGVGKS
17
ALTIQLIQNH
27
FVDEYDPTIE
37
DSYRKQVVID
47

GETCLLDILD
57
TAGHEEYSAM
67
RDQYMRTGEG
77
FLCVFAINNT
87
KSFEDIHHYR
97

EQIKRVKDSE
107
DVPMVLVGNK
117
CDLPSRTVDT
127
KQAQDLARSY
137
GIPFIETSAK
147

TRQGVDDAFY
157
TLVREIRKHK
167
E
> Chain B
AFQGMTEYKL
6
VVVGAGGVGK
16
SALTIQLIQN
26
HFVDEYDPTI
36
EDSYRKQVVI
46

DGETLLDILD
57
TAGHEEYSAM
67
RDQYMRTGEG
77
FLCVFAINNT
87
KSFEDIHHYR
97

EQIKRVKDSE
107
DVPMVLVGNK
117
CDLPSRTVDT
127
KQAQDLARSY
137
GIPFIETSAK
147

TRQGVDDAFY
157
TLVREIRKHK
167
E
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:10 or .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147 or .B:10 or .B:11 or .B:12 or .B:13 or .B:14 or .B:15 or .B:16 or .B:17 or .B:18 or .B:28 or .B:29 or .B:30 or .B:31 or .B:32 or .B:33 or .B:34 or .B:35 or .B:57 or .B:58 or .B:59 or .B:60 or .B:116 or .B:117 or .B:118 or .B:119 or .B:120 or .B:144 or .B:145 or .B:146 or .B:147; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue [Chain]
Distance (Å)
GLY10[A]
4.772
ALA11[A]
3.870
GLY12[A]
3.574
GLY13[A]
3.071
VAL14[A]
3.258
GLY15[A]
3.113
LYS16[A]
2.643
SER17[A]
2.913
ALA18[A]
2.730
PHE28[A]
3.435
VAL29[A]
2.681
ASP30[A]
2.828
GLU31[A]
3.565
TYR32[A]
3.648
ASP33[A]
4.298
PRO34[A]
3.379
THR35[A]
2.868
ASP57[A]
4.668
THR58[A]
4.117
ALA59[A]
3.810
GLY60[A]
2.763
ASN116[A]
3.126
LYS117[A]
3.253
CYS118[A]
4.821
ASP119[A]
2.791
LEU120[A]
3.477
THR144[A]
4.680
SER145[A]
3.456
ALA146[A]
2.911
LYS147[A]
3.650
Residue [Chain]
Distance (Å)
GLY10[B]
4.812
ALA11[B]
3.918
GLY12[B]
3.464
GLY13[B]
3.087
VAL14[B]
3.248
GLY15[B]
3.071
LYS16[B]
2.638
SER17[B]
2.995
ALA18[B]
2.722
PHE28[B]
3.379
VAL29[B]
2.587
ASP30[B]
2.892
GLU31[B]
3.518
TYR32[B]
3.590
ASP33[B]
4.315
PRO34[B]
3.376
THR35[B]
2.803
ASP57[B]
4.689
THR58[B]
4.116
ALA59[B]
3.944
GLY60[B]
2.913
ASN116[B]
3.071
LYS117[B]
3.156
CYS118[B]
4.779
ASP119[B]
2.791
LEU120[B]
3.412
THR144[B]
4.577
SER145[B]
3.399
ALA146[B]
2.815
LYS147[B]
3.703
PDB ID: 6GOF      KRAS full length G12D GPPNHP
Method X-ray diffraction Resolution 1.98 Å Mutation Yes [7]
PDB Sequence
STEYKLVVVG
10
ADGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHHYREQI
100

KRVKDSEDVP
110
MVLVGNKCDL
120
PSRTVDTKQA
130
QDLARSYGIP
140
FIETSAKTRQ
150

GVDDAFYTLV
160
REIRKHKEKM
170
SK
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:10 or .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:61 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY10
4.984
ALA11
3.790
ASP12
3.515
GLY13
3.171
VAL14
3.308
GLY15
3.071
LYS16
2.678
SER17
2.915
ALA18
2.824
PHE28
3.210
VAL29
2.863
ASP30
3.137
GLU31
3.485
TYR32
3.496
ASP33
4.472
PRO34
3.343
Residue
Distance (Å)
THR35
2.665
ASP57
4.785
THR58
4.082
ALA59
3.967
GLY60
2.861
GLN61
4.995
ASN116
3.137
LYS117
3.225
CYS118
4.975
ASP119
2.792
LEU120
3.636
THR144
4.707
SER145
3.384
ALA146
2.768
LYS147
3.377
PDB ID: 6GQT      KRAS-169 Q61H GPPNHP + PPIN-2
Method X-ray diffraction Resolution 1.69 Å Mutation Yes [7]
PDB Sequence
FQGMTEYKLV
7
VVGAGGVGKS
17
ALTIQLIQNH
27
FVDEYDPTIE
37
DSYRKQVVID
47

GETCLLDILD
57
TAGHEEYSAM
67
RDQYMRTGEG
77
FLCVFAINNT
87
KSFEDIHHYR
97

EQIKRVKDSE
107
DVPMVLVGNK
117
CDLPSRTVDT
127
KQAQDLARSY
137
GIPFIETSAK
147

TRQGVDDAFY
157
TLVREIRKHK
167
E
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:10 or .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:61 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY10
4.863
ALA11
3.980
GLY12
3.723
GLY13
3.156
VAL14
3.310
GLY15
3.065
LYS16
2.675
SER17
2.989
ALA18
2.835
PHE28
3.372
VAL29
2.716
ASP30
2.969
GLU31
3.573
TYR32
3.696
ASP33
4.376
PRO34
3.524
Residue
Distance (Å)
THR35
2.899
ASP57
4.830
THR58
4.113
ALA59
3.931
GLY60
2.873
HIS61
4.658
ASN116
3.081
LYS117
3.328
CYS118
4.848
ASP119
2.884
LEU120
3.550
THR144
4.734
SER145
3.501
ALA146
2.882
LYS147
3.753
PDB ID: 6GQX      KRAS-169 Q61H GPPNHP + CH-2
Method X-ray diffraction Resolution 2.20 Å Mutation Yes [7]
PDB Sequence
> Chain A
YFQGMTEYKL
6
VVVGAGGVGK
16
SALTIQLIQN
26
HFVDEYDPTI
36
EDSYRKQVVI
46

DGETCLLDIL
56
DTAGHEEYSA
66
MRDQYMRTGE
76
GFLCVFAINN
86
TKSFEDIHHY
96

REQIKRVKDS
106
EDVPMVLVGN
116
KCDLPSRTVD
126
TKQAQDLARS
136
YGIPFIETSA
146

KTRQGVDDAF
156
YTLVREIRKH
166
K
> Chain B
FQGMTEYKLV
7
VVGAGGVGKS
17
ALTIQLIQNH
27
FVDEYDPTIE
37
DSYRKQVVID
47

GETCLLDILD
57
TAGHEESAMR
68
DQYMRTGEGF
78
LCVFAINNTK
88
SFEDIHHYRE
98

QIKRVKDSED
108
VPMVLVGNKC
118
DLPSRTVDTK
128
QAQDLARSYG
138
IPFIETSAKT
148

RQGVDDAFYT
158
LVREIRKHK
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:10 or .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:61 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147 or .B:10 or .B:11 or .B:12 or .B:13 or .B:14 or .B:15 or .B:16 or .B:17 or .B:18 or .B:28 or .B:29 or .B:30 or .B:31 or .B:32 or .B:33 or .B:34 or .B:35 or .B:57 or .B:58 or .B:59 or .B:60 or .B:61 or .B:116 or .B:117 or .B:118 or .B:119 or .B:120 or .B:144 or .B:145 or .B:146 or .B:147; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue [Chain]
Distance (Å)
GLY10[A]
4.900
ALA11[A]
3.810
GLY12[A]
3.720
GLY13[A]
3.104
VAL14[A]
3.304
GLY15[A]
3.076
LYS16[A]
2.649
SER17[A]
2.913
ALA18[A]
2.708
PHE28[A]
3.416
VAL29[A]
2.623
ASP30[A]
2.688
GLU31[A]
3.690
TYR32[A]
3.598
ASP33[A]
4.401
PRO34[A]
3.425
THR35[A]
2.950
ASP57[A]
4.653
THR58[A]
3.966
ALA59[A]
3.759
GLY60[A]
2.725
HIS61[A]
4.830
ASN116[A]
3.043
LYS117[A]
3.208
CYS118[A]
4.821
ASP119[A]
2.718
LEU120[A]
3.590
THR144[A]
4.637
SER145[A]
3.401
ALA146[A]
2.819
LYS147[A]
3.762
Residue [Chain]
Distance (Å)
GLY10[B]
4.992
ALA11[B]
3.867
GLY12[B]
3.446
GLY13[B]
3.077
VAL14[B]
3.297
GLY15[B]
3.042
LYS16[B]
2.742
SER17[B]
2.936
ALA18[B]
2.770
PHE28[B]
3.479
VAL29[B]
2.568
ASP30[B]
2.620
GLU31[B]
3.549
TYR32[B]
3.605
ASP33[B]
4.241
PRO34[B]
3.220
THR35[B]
3.074
ASP57[B]
4.606
THR58[B]
3.959
ALA59[B]
3.951
GLY60[B]
2.877
HIS61[B]
4.947
ASN116[B]
3.049
LYS117[B]
3.229
CYS118[B]
4.836
ASP119[B]
2.758
LEU120[B]
3.503
THR144[B]
4.672
SER145[B]
3.412
ALA146[B]
2.836
LYS147[B]
3.703
PDB ID: 6FA2      Antibody derived (Abd-5) small molecule binding to KRAS.
Method X-ray diffraction Resolution 2.60 Å Mutation Yes [1]
PDB Sequence
> Chain A
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
HEEYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHHYREQI
100

KRVKDSEDVP
110
MVLVGNKCDL
120
PSRTVDTKQA
130
QDLARSYGIP
140
FIETSAKTRQ
150

GVDDAFYTLV
160
REIRKHK
> Chain B
FQGMTEYKLV
7
VVGAGGVGKS
17
ALTIQLIQNH
27
FVDEYDPTIE
37
DSYRKQVVID
47

GETCLLDILD
57
TAGHESAMRD
69
QYMRTGEGFL
79
CVFAINNTKS
89
FEDIHHYREQ
99

IKRVKDSEDV
109
PMVLVGNKCD
119
LPSRTVDTKQ
129
AQDLARSYGI
139
PFIETSAKTR
149

QGVDDAFYTL
159
VREIRKHK
> Chain C
YFQGMTEYKL
6
VVVGAGGVGK
16
SALTIQLIQN
26
HFVDEYDPTD
38
SYRKQVVIDG
48

ETCLLDILDT
58
AGSAMRDQYM
72
RTGEGFLCVF
82
AINNTKSFED
92
IHHYREQIKR
102

VKDSEDVPMV
112
LVGNKCDLPS
122
RTVDTKQAQD
132
LARSYGIPFI
142
ETSAKTRQGV
152

DDAFYTLVRE
162
IRKHK
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:10 or .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:61 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147 or .B:10 or .B:11 or .B:12 or .B:13 or .B:14 or .B:15 or .B:16 or .B:17 or .B:18 or .B:28 or .B:29 or .B:30 or .B:31 or .B:32 or .B:33 or .B:34 or .B:35 or .B:57 or .B:58 or .B:59 or .B:60 or .B:61 or .B:116 or .B:117 or .B:119 or .B:120 or .B:144 or .B:145 or .B:146 or .B:147 or .C:10 or .C:11 or .C:12 or .C:13 or .C:14 or .C:15 or .C:16 or .C:17 or .C:18 or .C:28 or .C:29 or .C:30 or .C:31 or .C:32 or .C:33 or .C:34 or .C:35 or .C:57 or .C:58 or .C:59 or .C:60 or .C:116 or .C:117 or .C:118 or .C:119 or .C:120 or .C:144 or .C:145 or .C:146 or .C:147; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue [Chain]
Distance (Å)
GLY10[A]
4.914
ALA11[A]
3.813
GLY12[A]
3.781
GLY13[A]
3.241
VAL14[A]
3.536
GLY15[A]
3.090
LYS16[A]
2.533
SER17[A]
2.964
ALA18[A]
2.701
PHE28[A]
3.375
VAL29[A]
2.888
ASP30[A]
2.598
GLU31[A]
3.831
TYR32[A]
3.417
ASP33[A]
4.368
PRO34[A]
3.631
THR35[A]
2.806
ASP57[A]
4.771
THR58[A]
4.229
ALA59[A]
3.955
GLY60[A]
3.066
HIS61[A]
4.796
ASN116[A]
2.873
LYS117[A]
3.155
CYS118[A]
4.868
ASP119[A]
2.708
LEU120[A]
3.364
THR144[A]
4.630
SER145[A]
3.362
ALA146[A]
2.859
LYS147[A]
3.613
GLY10[B]
4.966
ALA11[B]
3.779
GLY12[B]
3.608
GLY13[B]
3.316
VAL14[B]
3.304
GLY15[B]
2.957
LYS16[B]
2.665
SER17[B]
2.942
ALA18[B]
2.824
PHE28[B]
3.436
VAL29[B]
2.607
ASP30[B]
2.905
GLU31[B]
4.005
TYR32[B]
3.477
ASP33[B]
4.400
Residue [Chain]
Distance (Å)
PRO34[B]
3.527
THR35[B]
2.967
ASP57[B]
4.520
THR58[B]
4.073
ALA59[B]
4.110
GLY60[B]
3.178
HIS61[B]
4.745
ASN116[B]
3.047
LYS117[B]
3.053
ASP119[B]
2.758
LEU120[B]
3.394
THR144[B]
4.724
SER145[B]
3.537
ALA146[B]
2.832
LYS147[B]
3.723
GLY10[C]
4.847
ALA11[C]
3.985
GLY12[C]
3.257
GLY13[C]
3.223
VAL14[C]
3.470
GLY15[C]
3.000
LYS16[C]
2.747
SER17[C]
3.014
ALA18[C]
2.779
PHE28[C]
3.239
VAL29[C]
2.974
ASP30[C]
2.972
GLU31[C]
4.135
TYR32[C]
3.443
ASP33[C]
4.353
PRO34[C]
3.290
THR35[C]
3.211
ASP57[C]
4.775
THR58[C]
3.476
ALA59[C]
3.964
GLY60[C]
2.951
ASN116[C]
2.778
LYS117[C]
2.954
CYS118[C]
4.695
ASP119[C]
2.673
LEU120[C]
3.561
THR144[C]
4.429
SER145[C]
3.247
ALA146[C]
2.894
LYS147[C]
3.736
PDB ID: 6GQY      KRAS-169 Q61H GPPNHP + CH-3
Method X-ray diffraction Resolution 2.75 Å Mutation Yes [7]
PDB Sequence
YFQGMTEYKL
6
VVVGAGGVGK
16
SALTIQLIQN
26
HFVDEYDPTI
36
EDSYRKQVVI
46

DGETCLLDIL
56
DTAGHEEYSA
66
MRDQYMRTGE
76
GFLCVFAINN
86
TKSFEDIHHY
96

REQIKRVKDS
106
EDVPMVLVGN
116
KCDLPSRTVD
126
TKQAQDLARS
136
YGIPFIETSA
146

KTRQGVDDAF
156
YTLVREIRKH
166
K
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:10 or .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:61 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY10
4.848
ALA11
3.836
GLY12
3.474
GLY13
3.217
VAL14
3.303
GLY15
3.052
LYS16
2.576
SER17
2.754
ALA18
2.766
PHE28
3.518
VAL29
2.647
ASP30
2.688
GLU31
3.768
TYR32
3.665
ASP33
4.379
PRO34
3.670
Residue
Distance (Å)
THR35
2.780
ASP57
4.580
THR58
4.101
ALA59
4.226
GLY60
3.277
HIS61
4.965
ASN116
2.980
LYS117
3.357
CYS118
4.921
ASP119
2.733
LEU120
3.489
THR144
4.576
SER145
3.425
ALA146
2.812
LYS147
3.690
PDB ID: 6GQW      KRAS-169 Q61H GPPNHP + CH-1
Method X-ray diffraction Resolution 2.80 Å Mutation Yes [7]
PDB Sequence
> Chain A
FQGMTEYKLV
7
VVGAGGVGKS
17
ALTIQLIQNH
27
FVDEYDPTIE
37
DSYRKQVVID
47

GETCLLDILD
57
TAGHEEYSAM
67
RDQYMRTGEG
77
FLCVFAINNT
87
KSFEDIHHYR
97

EQIKRVKDSE
107
DVPMVLVGNK
117
CDLPSRTVDT
127
KQAQDLARSY
137
GIPFIETSAK
147

TRQGVDDAFY
157
TLVREIRKHK
167

> Chain E
YFQGMTEYKL
6
VVVGAGGVGK
16
SALVIQLIQN
26
HFVDEYDPED
38
SYRKQVVIDG
48

ETCLLDILDT
58
AGRDQYMRTG
75
EGFLCVFAIN
85
NTKSFEDIHH
95
YREQIKRVKD
105

SEDVPMVLVG
115
NKCDLPSRTV
125
DTKQAQDLAR
135
SYGIPFIETS
145
AKTRQGVDDA
155

FYTLVREIRK
165
HK
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:10 or .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:61 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147 or .E:10 or .E:11 or .E:12 or .E:13 or .E:14 or .E:15 or .E:16 or .E:17 or .E:18 or .E:28 or .E:29 or .E:30 or .E:31 or .E:32 or .E:33 or .E:34 or .E:57 or .E:58 or .E:59 or .E:60 or .E:116 or .E:117 or .E:118 or .E:119 or .E:120 or .E:144 or .E:145 or .E:146 or .E:147; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue [Chain]
Distance (Å)
GLY10[A]
4.843
ALA11[A]
3.891
GLY12[A]
3.498
GLY13[A]
3.177
VAL14[A]
3.466
GLY15[A]
3.118
LYS16[A]
2.520
SER17[A]
2.887
ALA18[A]
2.775
PHE28[A]
3.284
VAL29[A]
2.786
ASP30[A]
2.610
GLU31[A]
3.711
TYR32[A]
3.698
ASP33[A]
4.421
PRO34[A]
3.540
THR35[A]
2.693
ASP57[A]
4.700
THR58[A]
4.112
ALA59[A]
4.155
GLY60[A]
3.185
HIS61[A]
4.867
ASN116[A]
3.039
LYS117[A]
3.220
CYS118[A]
4.865
ASP119[A]
2.851
LEU120[A]
3.514
THR144[A]
4.636
SER145[A]
3.412
ALA146[A]
2.754
Residue [Chain]
Distance (Å)
LYS147[A]
3.730
GLY10[E]
4.890
ALA11[E]
3.940
GLY12[E]
3.190
GLY13[E]
3.064
VAL14[E]
3.462
GLY15[E]
2.999
LYS16[E]
2.849
SER17[E]
2.994
ALA18[E]
2.890
PHE28[E]
3.447
VAL29[E]
2.889
ASP30[E]
2.956
GLU31[E]
4.022
TYR32[E]
3.619
ASP33[E]
4.460
PRO34[E]
3.375
ASP57[E]
4.932
THR58[E]
3.895
ALA59[E]
4.065
GLY60[E]
2.976
ASN116[E]
3.118
LYS117[E]
3.088
CYS118[E]
4.931
ASP119[E]
2.713
LEU120[E]
3.616
THR144[E]
4.631
SER145[E]
3.409
ALA146[E]
2.767
LYS147[E]
3.705
PDB ID: 6VJJ      Crystal Structure of wild-type KRAS4b (GMPPNP-bound) in complex with RAS-binding domain (RBD) of RAF1/CRAF
Method X-ray diffraction Resolution 1.40 Å Mutation No [9]
PDB Sequence
GMTEYKLVVV
9
GAGGVGKSAL
19
TIQLIQNHFV
29
DEYDPTIEDS
39
YRKQVVIDGE
49

TCLLDILDTA
59
GQEEYSAMRD
69
QYMRTGEGFL
79
CVFAINNTKS
89
FEDIHHYREQ
99

IKRVKDSEDV
109
PMVLVGNKCD
119
LPSRTVDTKQ
129
AQDLARSYGI
139
PFIETSAKTR
149

QGVDDAFYTL
159
VREIRKHK
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:10 or .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:61 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY10
4.718
ALA11
3.884
GLY12
3.407
GLY13
3.096
VAL14
3.201
GLY15
2.997
LYS16
2.658
SER17
2.955
ALA18
2.772
LEU19
4.984
PHE28
3.352
VAL29
2.652
ASP30
2.889
GLU31
3.363
TYR32
3.633
ASP33
4.322
Residue
Distance (Å)
PRO34
3.363
THR35
2.861
ASP57
4.829
THR58
4.159
ALA59
3.959
GLY60
2.768
GLN61
4.263
ASN116
3.084
LYS117
3.108
CYS118
4.781
ASP119
2.772
LEU120
3.578
THR144
4.707
SER145
3.442
ALA146
2.782
LYS147
3.538
PDB ID: 6CU6      Crystal structure of GMPPNP-bound G12R mutant of human KRAS4b
Method X-ray diffraction Resolution 1.50 Å Mutation Yes [10]
PDB Sequence
GMTEYKLVVV
9
GARGVGKSAL
19
TIQLIQNHFV
29
DEYDPTIEDS
39
YRKQVVIDGE
49

TCLLDILDTA
59
GQEEAMRDQY
71
MRTGEGFLCV
81
FAINNTKSFE
91
DIHHYREQIK
101

RVKDSEDVPM
111
VLVGNKCDLP
121
SRTVDTKQAQ
131
DLARSYGIPF
141
IETSAKTRQG
151

VDDAFYTLVR
161
EIRKHKE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:10 or .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY10
4.978
ALA11
3.939
ARG12
2.788
GLY13
3.137
VAL14
3.183
GLY15
2.967
LYS16
2.690
SER17
2.889
ALA18
2.718
LEU19
4.965
PHE28
3.414
VAL29
2.680
ASP30
2.946
GLU31
3.501
TYR32
2.489
ASP33
4.449
Residue
Distance (Å)
PRO34
3.710
THR35
3.018
ASP57
4.757
THR58
4.326
ALA59
3.998
GLY60
2.829
ASN116
3.147
LYS117
3.186
CYS118
4.862
ASP119
2.722
LEU120
3.291
THR144
4.716
SER145
3.430
ALA146
2.831
LYS147
3.711
PDB ID: 5WHE      KRas G12V/D38P, bound to GppNHp and miniprotein 225-11
Method X-ray diffraction Resolution 1.91 Å Mutation Yes [11]
PDB Sequence
TEYKLVVVGA
11
VGVGKSALTI
21
QLIQNHFVDE
31
YDPEPSYRKQ
43
VVIDGETCLL
53

DILDTAGQEE
63
YSAMRDQYMR
73
TGEGFLCVFA
83
INNTKSFEDI
93
HHYREQIKRV
103

KDSEDVPMVL
113
VGNKCDLPSR
123
TVDTKQAQDL
133
ARSYGIPFIE
143
TSAKTRQGVD
153

DAFYTLVREI
163
RKH
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:28 or .A:57 or .A:58 or .A:59 or .A:60 or .A:61 or .A:116 or .A:117 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ALA11
4.039
VAL12
3.315
GLY13
3.284
VAL14
3.328
GLY15
3.096
LYS16
2.694
SER17
3.023
ALA18
2.827
PHE28
3.266
ASP57
4.637
THR58
4.568
Residue
Distance (Å)
ALA59
4.482
GLY60
3.151
GLN61
4.712
ASN116
3.261
LYS117
3.024
ASP119
2.713
LEU120
3.414
THR144
4.815
SER145
3.447
ALA146
2.659
LYS147
3.376
PDB ID: 6XI7      Crystal Structure of wild-type KRAS (GMPPNP-bound) in complex with RAS-binding domain (RBD) and cysteine-rich domain (CRD) of RAF1/CRAF (crystal form I)
Method X-ray diffraction Resolution 1.95 Å Mutation Yes [9]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHHYREQI
100

KRVKDSEDVP
110
MVLVGNKSDL
120
PSRTVDTKQA
130
QDLARSYGIP
140
FIETSAKTRQ
150

GVDDAFYTLV
160
REIRKHKEK
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:10 or .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY10
4.873
ALA11
3.820
GLY12
3.486
GLY13
3.071
VAL14
3.190
GLY15
3.059
LYS16
2.733
SER17
2.896
ALA18
2.766
PHE28
3.270
VAL29
2.811
ASP30
3.005
GLU31
3.274
TYR32
3.837
ASP33
4.372
Residue
Distance (Å)
PRO34
3.399
THR35
2.870
ASP57
4.743
THR58
4.052
ALA59
3.958
GLY60
2.950
ASN116
3.202
LYS117
3.137
SER118
4.906
ASP119
2.768
LEU120
3.589
THR144
4.901
SER145
3.524
ALA146
2.782
LYS147
3.279
PDB ID: 6OB3      Crystal structure of G13D-KRAS (GMPPNP-bound) in complex with GAP-related domain (GRD) of neurofibromin (NF1)
Method X-ray diffraction Resolution 2.10 Å Mutation Yes [12]
PDB Sequence
GMTEYKLVVV
9
GAGDVGKSAL
19
TIQLIQNHFV
29
DEYDPTIEDS
39
YRKQVVIDGE
49

TCLLDILDTA
59
GQEEYSAMRD
69
QYMRTGEGFL
79
CVFAINNTKS
89
FEDIHHYREQ
99

IKRVKDSEDV
109
PMVLVGNKCD
119
LPSRTVDTKQ
129
AQDLARSYGI
139
PFIETSAKTR
149

QGVDDAFYTL
159
VREIRKHKEK
169
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:10 or .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:28 or .A:29 or .A:30 or .A:31 or .A:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:61 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY10
4.776
ALA11
3.701
GLY12
3.535
ASP13
3.160
VAL14
3.303
GLY15
3.017
LYS16
2.697
SER17
2.928
ALA18
2.741
PHE28
3.249
VAL29
3.267
ASP30
3.310
GLU31
4.128
ASP33
4.547
PRO34
3.525
Residue
Distance (Å)
THR35
2.853
ASP57
4.806
THR58
4.243
ALA59
3.985
GLY60
2.809
GLN61
3.177
ASN116
3.250
LYS117
3.320
CYS118
4.977
ASP119
2.787
LEU120
3.733
THR144
4.789
SER145
3.464
ALA146
2.794
LYS147
3.285
PDB ID: 6XGV      Crystal Structure of KRAS-G13D (GMPPNP-bound) in complex with RAS-binding domain (RBD) and cysteine-rich domain (CRD) of RAF1/CRAF
Method X-ray diffraction Resolution 2.11 Å Mutation Yes [9]
PDB Sequence
MTEYKLVVVG
10
AGDVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHHYREQI
100

KRVKDSEDVP
110
MVLVGNKCDL
120
PSRTVDTKQA
130
QDLARSYGIP
140
FIETSAKTRQ
150

GVDDAFYTLV
160
REIRKHKE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:10 or .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:61 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY10
4.993
ALA11
3.914
GLY12
3.700
ASP13
3.054
VAL14
3.431
GLY15
3.075
LYS16
2.835
SER17
2.992
ALA18
2.708
LEU19
4.956
PHE28
3.408
VAL29
3.070
ASP30
2.753
GLU31
4.145
TYR32
4.205
ASP33
4.243
Residue
Distance (Å)
PRO34
4.236
THR35
3.051
ASP57
4.741
THR58
4.023
ALA59
4.176
GLY60
3.469
GLN61
3.743
ASN116
3.177
LYS117
3.328
CYS118
4.846
ASP119
2.907
LEU120
3.449
THR144
4.787
SER145
3.412
ALA146
2.793
LYS147
3.413
PDB ID: 7LC1      Crystal Structure of KRAS4b (GMPPNP-bound) in complex with the RBD-PH domains of SIN1
Method X-ray diffraction Resolution 2.35 Å Mutation Yes [13]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIANHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHHYREQI
100

KRVKDSEDVP
110
MVLVGNKCDL
120
PSRTVDTKQA
130
QDLARSYGIP
140
FIETSAKTRQ
150

GVDDAFYTLV
160
REIRKHK
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:10 or .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:61 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY10
4.982
ALA11
3.795
GLY12
3.511
GLY13
3.112
VAL14
3.205
GLY15
3.060
LYS16
2.695
SER17
2.618
ALA18
2.709
PHE28
3.213
VAL29
2.881
ASP30
2.924
GLU31
3.704
TYR32
3.147
ASP33
4.309
PRO34
3.477
Residue
Distance (Å)
THR35
2.581
ASP57
4.753
THR58
4.377
ALA59
4.051
GLY60
2.902
GLN61
4.553
ASN116
2.994
LYS117
3.078
CYS118
4.839
ASP119
2.835
LEU120
3.701
THR144
4.811
SER145
3.449
ALA146
2.808
LYS147
3.518
PDB ID: 6VC8      Crystal structure of wild-type KRAS4b(1-169) in complex with GMPPNP and Mg ion
Method X-ray diffraction Resolution 2.50 Å Mutation No [14]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QQYMRTGEGF
78
LCVFAINNTK
88
SFEDIHHYRE
98
QIKRVKDSED
108

VPMVLVGNKC
118
DLPSRTVDTK
128
QAQDLARSYG
138
IPFIETSAKT
148
RQGVDDAFYT
158

LVREIRKHKE
168
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:10 or .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY10
4.892
ALA11
3.890
GLY12
3.070
GLY13
3.132
VAL14
3.063
GLY15
2.783
LYS16
2.773
SER17
2.782
ALA18
2.734
PHE28
3.229
VAL29
3.017
ASP30
3.235
GLU31
4.615
TYR32
2.755
ASP33
4.421
Residue
Distance (Å)
PRO34
3.648
THR35
3.248
ASP57
4.556
THR58
4.332
ALA59
4.307
GLY60
3.536
ASN116
3.307
LYS117
3.365
CYS118
4.845
ASP119
2.881
LEU120
3.187
THR144
4.857
SER145
3.235
ALA146
2.901
LYS147
3.335
PDB ID: 6XHB      Crystal Structure of wild-type KRAS (GMPPNP-bound) in complex with RAS-binding domain (RBD) and cysteine-rich domain (CRD) of RAF1/CRAF (crystal form II)
Method X-ray diffraction Resolution 2.50 Å Mutation No [9]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEAMRDQYM
72
RTGEGFLCVF
82
AINNTKSFED
92
IHHYREQIKR
102

VKDSEDVPMV
112
LVGNKCDLPS
122
RTVDTKQAQD
132
LARSYGIPFI
142
ETSAKTRQGV
152

DDAFYTLVRE
162
IRKHKE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:61 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ALA11
3.852
GLY12
3.386
GLY13
3.047
VAL14
3.085
GLY15
2.939
LYS16
2.797
SER17
2.868
ALA18
2.722
PHE28
3.425
VAL29
2.857
ASP30
3.187
GLU31
3.506
TYR32
3.580
ASP33
4.241
PRO34
3.387
Residue
Distance (Å)
THR35
2.908
ASP57
4.748
THR58
4.219
ALA59
4.157
GLY60
3.035
GLN61
4.464
ASN116
3.134
LYS117
3.324
CYS118
4.750
ASP119
2.756
LEU120
3.358
THR144
4.782
SER145
3.373
ALA146
2.822
LYS147
3.548
PDB ID: 6V6F      Crystal structure of Q61L KRAS(GMPPNP)-NF1(GRD)-SPRED1(EVH1) complex
Method X-ray diffraction Resolution 2.54 Å Mutation Yes [15]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
LEEYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHHYREQI
100

KRVKDSEDVP
110
MVLVGNKCDL
120
PSRTVDTKQA
130
QDLARSYGIP
140
FIETSAKTRQ
150

GVDDAFYTLV
160
REIRKHKE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .C:11 or .C:12 or .C:13 or .C:14 or .C:15 or .C:16 or .C:17 or .C:18 or .C:28 or .C:29 or .C:30 or .C:31 or .C:32 or .C:33 or .C:34 or .C:35 or .C:57 or .C:58 or .C:59 or .C:60 or .C:61 or .C:116 or .C:117 or .C:118 or .C:119 or .C:120 or .C:145 or .C:146 or .C:147; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ALA11
4.105
GLY12
3.836
GLY13
3.124
VAL14
3.306
GLY15
2.997
LYS16
2.695
SER17
3.068
ALA18
2.822
PHE28
3.364
VAL29
3.375
ASP30
3.491
GLU31
3.351
TYR32
3.675
ASP33
4.115
PRO34
3.413
Residue
Distance (Å)
THR35
2.516
ASP57
4.864
THR58
4.107
ALA59
3.922
GLY60
2.768
LEU61
4.048
ASN116
3.143
LYS117
3.331
CYS118
4.844
ASP119
2.826
LEU120
3.534
SER145
3.542
ALA146
2.953
LYS147
3.455
PDB ID: 6XGU      Crystal Structure of KRAS-Q61R (GMPPNP-bound) in complex with RAS-binding domain (RBD) and cysteine-rich domain (CRD) of RAF1/CRAF
Method X-ray diffraction Resolution 2.70 Å Mutation Yes [9]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
REEYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHHYREQI
100

KRVKDSEDVP
110
MVLVGNKCDL
120
PSRTVDTKQA
130
QDLARSYGIP
140
FIETSAKTRQ
150

GVDDAFYTLV
160
REIRKHKE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:10 or .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:61 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY10
4.878
ALA11
3.746
GLY12
3.496
GLY13
3.050
VAL14
3.185
GLY15
3.016
LYS16
2.639
SER17
2.882
ALA18
2.618
LEU19
4.897
PHE28
3.889
VAL29
2.955
ASP30
3.159
GLU31
3.256
TYR32
4.548
ASP33
4.323
Residue
Distance (Å)
PRO34
3.337
THR35
2.854
ASP57
4.629
THR58
4.271
ALA59
4.151
GLY60
3.032
ARG61
4.442
ASN116
3.054
LYS117
2.951
CYS118
4.658
ASP119
2.711
LEU120
3.760
THR144
4.840
SER145
3.451
ALA146
2.750
LYS147
3.458
PDB ID: 7LC2      Crystal Structure of KRAS4b-Q61R (GMPPNP-bound) in complex with the RAS-binding domain (RBD) of SIN1
Method X-ray diffraction Resolution 2.70 Å Mutation Yes [13]
PDB Sequence
GTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
REEYSARDQY
71
RTGEGFLCVF
82
AINNTKSFED
92
IHHYREQIKR
102

VKDSEDVPVL
113
VGNKCDLPSR
123
TVDTKQAQDL
133
ARSYGIPFIE
143
TSAKTRQGVD
153

DAFYTLVREI
163
RKH
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:61 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ALA11
3.795
GLY12
3.694
GLY13
2.931
VAL14
3.207
GLY15
2.961
LYS16
2.813
SER17
2.599
ALA18
2.738
PHE28
3.173
VAL29
3.200
ASP30
2.724
GLU31
4.726
TYR32
3.028
ASP33
4.483
PRO34
3.789
Residue
Distance (Å)
THR35
2.839
ASP57
4.828
THR58
4.114
ALA59
3.888
GLY60
2.800
ARG61
4.309
ASN116
3.070
LYS117
2.856
CYS118
4.731
ASP119
3.004
LEU120
3.657
THR144
4.964
SER145
3.454
ALA146
2.757
LYS147
3.340
PDB ID: 6V65      Crystal structure of KRAS(GMPPNP)-NF1(GRD)-SPRED1 complex
Method X-ray diffraction Resolution 2.76 Å Mutation No [15]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHHYREQI
100

KRVKDSEDVP
110
MVLVGNKCDL
120
PSRTVDTKQA
130
QDLARSYGIP
140
FIETSAKTRQ
150

GVDDAFYTLV
160
REIRKHKE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .C:11 or .C:12 or .C:13 or .C:14 or .C:15 or .C:16 or .C:17 or .C:18 or .C:19 or .C:28 or .C:29 or .C:30 or .C:31 or .C:32 or .C:33 or .C:34 or .C:35 or .C:58 or .C:59 or .C:60 or .C:61 or .C:116 or .C:117 or .C:118 or .C:119 or .C:120 or .C:145 or .C:146 or .C:147; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ALA11
4.082
GLY12
3.765
GLY13
3.277
VAL14
3.832
GLY15
3.172
LYS16
2.587
SER17
2.950
ALA18
2.682
LEU19
4.996
PHE28
3.647
VAL29
3.332
ASP30
3.557
GLU31
3.525
TYR32
3.793
ASP33
4.201
Residue
Distance (Å)
PRO34
3.329
THR35
2.784
THR58
4.188
ALA59
4.168
GLY60
2.984
GLN61
3.965
ASN116
3.242
LYS117
3.439
CYS118
4.862
ASP119
2.598
LEU120
3.552
SER145
3.421
ALA146
2.722
LYS147
3.348
PDB ID: 6OB2      Crystal structure of wild-type KRAS (GMPPNP-bound) in complex with GAP-related domain (GRD) of neurofibromin (NF1)
Method X-ray diffraction Resolution 2.85 Å Mutation No [12]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHHYREQI
100

KRVKDSEDVP
110
MVLVGNKCDL
120
PSRTVDTKQA
130
QDLARSYGIP
140
FIETSAKTRQ
150

GVDDAFYTLV
160
REIRKHKEK
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:10 or .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:61 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY10
4.579
ALA11
3.823
GLY12
3.485
GLY13
3.111
VAL14
3.525
GLY15
3.087
LYS16
2.537
SER17
2.785
ALA18
2.751
PHE28
3.163
VAL29
2.850
ASP30
3.401
GLU31
3.583
TYR32
3.795
ASP33
4.432
PRO34
3.559
Residue
Distance (Å)
THR35
2.934
ASP57
4.837
THR58
4.229
ALA59
4.155
GLY60
3.010
GLN61
4.248
ASN116
3.190
LYS117
3.369
CYS118
4.844
ASP119
2.776
LEU120
3.686
THR144
4.843
SER145
3.477
ALA146
2.833
LYS147
3.454
PDB ID: 6XHA      Crystal Structure of KRAS-G12V (GMPPNP-bound) in complex with RAS-binding domain (RBD) and cysteine-rich domain (CRD) of RAF1/CRAF
Method X-ray diffraction Resolution 2.87 Å Mutation Yes [9]
PDB Sequence
MTEYKLVVVG
10
AVGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHHYREQI
100

KRVKDSEDVP
110
MVLVGNKSDL
120
PSRTVDTKQA
130
QDLARSYGIP
140
FIETSAKTRQ
150

GVDDAFYTLV
160
REIRKHKE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:61 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:145 or .A:146 or .A:147; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ALA11
3.789
VAL12
3.888
GLY13
3.415
VAL14
3.300
GLY15
2.852
LYS16
2.666
SER17
2.718
ALA18
2.802
LEU19
4.881
PHE28
3.699
VAL29
3.080
ASP30
2.779
GLU31
4.656
TYR32
2.514
ASP33
4.005
Residue
Distance (Å)
PRO34
3.306
THR35
2.618
ASP57
4.846
THR58
4.502
ALA59
4.630
GLY60
3.514
GLN61
4.383
ASN116
3.195
LYS117
3.108
SER118
4.841
ASP119
2.753
LEU120
3.519
SER145
3.208
ALA146
2.411
LYS147
3.759
PDB ID: 6WGN      Crystal structure of K-Ras(G12D) GppNHp bound to cyclic peptide ligand KD2
Method X-ray diffraction Resolution 1.60 Å Mutation Yes [16]
PDB Sequence
MTEYKLVVVG
10
ADGVGKSALT
20
IQLIQNHFVD
30
EYDPDSYRKQ
43
VVIDGETSLL
53

DILDTAGQEE
63
YSAMRDQYMR
73
TGEGFLLVFA
83
INNTKSFEDI
93
HHYREQIKRV
103

KDSEDVPMVL
113
VGNKSDLPSR
123
TVDTKQAQDL
133
ARSYGIPFIE
143
TSAKTRQGVD
153

DAFYTLVREI
163
RKHKEK
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:57 or .A:58 or .A:59 or .A:60 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ALA11
4.070
ASP12
3.463
GLY13
3.222
VAL14
3.220
GLY15
3.084
LYS16
2.653
SER17
2.816
ALA18
2.688
PHE28
3.355
VAL29
2.497
ASP30
3.301
GLU31
3.593
TYR32
2.716
ASP33
4.312
Residue
Distance (Å)
PRO34
4.368
ASP57
4.650
THR58
4.376
ALA59
3.734
GLY60
4.911
ASN116
3.070
LYS117
3.185
SER118
4.767
ASP119
2.714
LEU120
3.536
THR144
4.607
SER145
3.433
ALA146
2.798
LYS147
3.452
PDB ID: 6O46      Crystal structure of human KRAS P34R mutant in complex with GNP and Phosphate
Method X-ray diffraction Resolution 1.90 Å Mutation Yes [17]
PDB Sequence
GMTEYKLVVV
9
GAGGVGKSAL
19
TIQLIQNHFV
29
DEYDRTIEDS
39
YRKQVVIDGE
49

TCLLDILDTA
59
GQEEYSAMRD
69
QYMRTGEGFL
79
CVFAINNTKS
89
FEDIHHYREQ
99

IKRVKDSEDV
109
PMVLVGNKCD
119
LPSRTVDTKQ
129
AQDLARSYGI
139
PFIETSAKTR
149

QGVDDAFYTL
159
VREIRKHKE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:10 or .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:28 or .A:29 or .A:30 or .A:34 or .A:57 or .A:58 or .A:59 or .A:60 or .A:61 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY10
4.856
ALA11
3.970
GLY12
3.423
GLY13
3.157
VAL14
3.254
GLY15
3.099
LYS16
2.688
SER17
2.942
ALA18
2.821
PHE28
3.328
VAL29
2.839
ASP30
2.977
ARG34
4.197
ASP57
4.519
Residue
Distance (Å)
THR58
4.202
ALA59
3.794
GLY60
2.666
GLN61
2.824
ASN116
3.134
LYS117
3.193
CYS118
4.842
ASP119
2.772
LEU120
3.487
THR144
4.705
SER145
3.435
ALA146
2.864
LYS147
3.455
PDB ID: 6MTA      KRAS P34R mutant structure in complex with GTP analogue
Method X-ray diffraction Resolution 2.15 Å Mutation Yes [17]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDRTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
RDQYMRTGEG
77
FLCVFAINNT
87
KSFEDIHHYR
97
EQIKRVKDSE
107

DVPMVLVGNK
117
CDLPSRTVDT
127
KQAQDLARSY
137
GIPFIETSAK
147
TRQGVDDAFY
157

TLVREIRKHK
167
E
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:10 or .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY10
4.811
ALA11
3.979
GLY12
3.363
GLY13
3.006
VAL14
3.345
GLY15
3.155
LYS16
2.623
SER17
2.909
ALA18
2.802
PHE28
3.279
VAL29
3.000
ASP30
2.935
GLU31
3.946
TYR32
2.645
ASP33
4.386
Residue
Distance (Å)
ARG34
4.535
THR35
3.210
ASP57
4.498
THR58
4.480
ALA59
3.843
GLY60
2.926
ASN116
3.061
LYS117
3.288
CYS118
4.903
ASP119
2.813
LEU120
3.442
THR144
4.690
SER145
3.403
ALA146
2.791
LYS147
3.588
PDB ID: 6O36      Crystal structure of human KRAS P34R mutant in complex with GNP
Method X-ray diffraction Resolution 2.00 Å Mutation Yes [17]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDRTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHHYREQI
100

KRVKDSEDVP
110
MVLVGNKCDL
120
PSRTVDTKQA
130
QDLARSYGIP
140
FIETSAKTRQ
150

GVDDAFYTLV
160
REIRKHKE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:10 or .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:28 or .A:29 or .A:30 or .A:57 or .A:58 or .A:59 or .A:60 or .A:61 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY10
4.902
ALA11
3.963
GLY12
3.447
GLY13
3.209
VAL14
3.472
GLY15
3.136
LYS16
2.670
SER17
2.870
ALA18
2.785
PHE28
3.198
VAL29
2.959
ASP30
2.974
ASP57
4.585
Residue
Distance (Å)
THR58
4.355
ALA59
3.843
GLY60
2.753
GLN61
2.481
ASN116
3.138
LYS117
3.282
CYS118
4.866
ASP119
2.835
LEU120
3.507
THR144
4.693
SER145
3.396
ALA146
2.874
LYS147
3.542
PDB ID: 6MBQ      Crystal structure of Mg-free wild-type KRAS (2-166) bound to GMPPNP in the state 1 conformation
Method X-ray diffraction Resolution 1.35 Å Mutation No [18]
PDB Sequence
GGTEYKLVVV
9
GAGGVGKSAL
19
TIQLIQNHFV
29
DEYDPTIEDS
39
YRKQVVIDGE
49

TCLLDILDTA
59
GQEEYSAMRD
69
QYMRTGEGFL
79
CVFAINNTKS
89
FEDIHHYREQ
99

IKRVKDSEDV
109
PMVLVGNKCD
119
LPSRTVDTKQ
129
AQDLARSYGI
139
PFIETSAKTR
149

QGVDDAFYTL
159
VREIRKH
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set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GNP or .GNP2 or .GNP3 or :3GNP;style chemicals stick;color identity;select .A:11 or .A:12 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:34 or .A:57 or .A:59 or .A:60 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146 or .A:147 or .A:148; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ALA11
3.789
GLY12
2.749
GLY13
2.104
VAL14
2.889
GLY15
2.332
LYS16
1.831
SER17
2.203
ALA18
1.920
LEU19
4.420
PHE28
2.796
VAL29
1.937
ASP30
2.291
GLU31
3.062
TYR32
3.139
Residue
Distance (Å)
PRO34
3.133
ASP57
4.674
ALA59
2.440
GLY60
3.475
ASN116
2.394
LYS117
2.519
CYS118
4.482
ASP119
1.942
LEU120
2.219
THR144
4.621
SER145
2.610
ALA146
2.210
LYS147
2.537
THR148
4.829
PDB ID: 5WLB      KRas G12V, bound to GppNHp and miniprotein 225-15a/b
Method X-ray diffraction Resolution 1.72 Å Mutation No [11]
PDB Sequence
MTEYKLVVVG
10
AVGVGKSALT
20
IQLIQNHFVD
30
DSYRKQVVID
47
GETCLLDILD
57

TAGQEEYSAM
67
RDQYMRTGEG
77
FLCVFAINNT
87
KSFEDIHHYR
97
EQIKRVKDSE
107

DVPMVLVGNK
117
CDLPSRTVDT
127
KQAQDLARSY
137
GIPFIETSAK
147
TRQGVDDAFY
157

TLVREIRKH
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Residue
Distance (Å)
GLY10
4.899
ALA11
3.919
VAL12
3.368
GLY13
3.163
VAL14
3.250
GLY15
2.929
LYS16
2.660
SER17
2.985
ALA18
2.806
PHE28
3.400
VAL29
3.720
ASP30
2.908
ASP57
4.668
Residue
Distance (Å)
THR58
4.322
ALA59
4.170
GLY60
3.012
GLN61
4.738
ASN116
3.156
LYS117
3.242
CYS118
4.843
ASP119
2.903
LEU120
3.764
THR144
4.624
SER145
3.360
ALA146
2.723
LYS147
3.463
PDB ID: 5WPM      KRas G12V, bound to GppNHp and miniprotein 225-11(A30R)
Method X-ray diffraction Resolution 1.72 Å Mutation Yes [11]
PDB Sequence
MTEYKLVVVG
10
AVGVGKSALT
20
IQLIQNHFDS
39
YRKQVVIDGE
49
TCLLDILDTA
59

GQEEYSAMRD
69
QYMRTGEGFL
79
CVFAINNTKS
89
FEDIHHYREQ
99
IKRVKDDVPM
111

VLVGNKCDLP
121
SRTVDTKQAQ
131
DLARSYGIPF
141
IETSAKTRQG
151
VDDAFYTLVR
161

EIR
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Residue
Distance (Å)
GLY10
4.642
ALA11
3.832
VAL12
3.588
GLY13
3.224
VAL14
3.462
GLY15
3.057
LYS16
2.560
SER17
2.830
ALA18
2.751
PHE28
3.223
ASP57
4.478
THR58
4.661
Residue
Distance (Å)
ALA59
3.948
GLY60
2.825
GLN61
3.250
ASN116
3.211
LYS117
3.122
CYS118
4.973
ASP119
2.759
LEU120
3.489
THR144
4.678
SER145
3.409
ALA146
2.848
LYS147
3.450
PDB ID: 5UFQ      K-RasG12D(GNP)/R11.1.6 complex
Method X-ray diffraction Resolution 2.20 Å Mutation Yes [19]
PDB Sequence
MTEYKLVVVG
10
ADGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHHYREQI
100

KRVKDSEDVP
110
MVLVGNKCDL
120
PSRTVDTKQA
130
QDLARSYGIP
140
FIETSAKTRQ
150

GVDDAFYTLV
160
REIRKH
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Residue
Distance (Å)
GLY10
4.980
ALA11
3.768
ASP12
2.744
GLY13
3.025
VAL14
3.329
GLY15
3.171
LYS16
2.518
SER17
2.983
ALA18
2.915
PHE28
3.191
VAL29
2.476
ASP30
3.216
GLU31
3.516
THR35
2.736
Residue
Distance (Å)
ASP57
4.728
THR58
4.481
ALA59
4.246
GLY60
3.058
GLN61
4.996
ASN116
3.298
LYS117
2.974
CYS118
4.872
ASP119
2.635
LEU120
3.530
THR144
4.706
SER145
3.469
ALA146
2.791
LYS147
3.372
PDB ID: 5UFE      Wild-type K-Ras(GNP)/R11.1.6 complex
Method X-ray diffraction Resolution 2.30 Å Mutation No [19]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHHYREQI
100

KRVKDSEDVP
110
MVLVGNKCDL
120
PSRTVDTKQA
130
QDLARSYGIP
140
FIETSAKTRQ
150

GVDDAFYTLV
160
REIRKH
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Residue
Distance (Å)
GLY10
4.885
ALA11
3.870
GLY12
3.723
GLY13
3.229
VAL14
3.381
GLY15
3.112
LYS16
2.536
SER17
2.790
ALA18
2.871
PHE28
3.729
ASP30
3.910
TYR32
4.055
ASP33
3.863
Residue
Distance (Å)
PRO34
4.154
ASP57
4.844
THR58
4.551
ALA59
4.565
GLY60
3.346
ASN116
3.034
LYS117
2.946
ASP119
2.781
LEU120
3.559
THR144
4.729
SER145
3.351
ALA146
2.680
LYS147
3.266
PDB ID: 6E6F      KRAS G13D bound to GppNHp (K13GNP)
Method X-ray diffraction Resolution 3.40 Å Mutation Yes [20]
PDB Sequence
MTEYKLVVVG
10
AGDVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTYM
72
RTGEGFLCVF
82
AINNTKSFED
92
IHHYREQIKR
102
VKDSEDVPMV
112

LVGNKCDLPS
122
RTVDTKQAQD
132
LARSYGIPFI
142
ETSAKTRQGV
152
DDAFYTLVRE
162

IRKH
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Residue
Distance (Å)
ALA11
3.953
GLY12
3.597
ASP13
2.949
VAL14
3.456
GLY15
3.007
LYS16
2.721
SER17
2.955
ALA18
2.541
LEU19
4.708
PHE28
3.322
VAL29
3.508
ASP30
2.688
Residue
Distance (Å)
GLU31
3.797
TYR32
3.006
THR58
4.837
ASN116
2.656
LYS117
3.255
CYS118
4.317
ASP119
2.920
LEU120
3.092
THR144
4.622
SER145
2.982
ALA146
2.966
LYS147
3.461
References  Top
REF 1 Small molecule inhibitors of RAS-effector protein interactions derived using an intracellular antibody fragment. Nat Commun. 2018 Aug 9;9(1):3169.
REF 2 Multivalent Small-Molecule Pan-RAS Inhibitors. Cell. 2017 Feb 23;168(5):878-889.e29.
REF 3 Structural insights into Ras regulation by SIN1. Proc Natl Acad Sci U S A. 2022 May 10;119(19):e2119990119.
REF 4 Inhibition of K-RAS4B by a Unique Mechanism of Action: Stabilizing Membrane-Dependent Occlusion of the Effector-Binding Site. Cell Chem Biol. 2018 Nov 15;25(11):1327-1336.e4.
REF 5 Human K-Ras (Q61H) in complex with a GTP analogue
REF 6 Multivalent assembly of KRAS with the RAS-binding and cysteine-rich domains of CRAF on the membrane. Proc Natl Acad Sci U S A. 2020 Jun 2;117(22):12101-12108.
REF 7 Structure-based development of new RAS-effector inhibitors from a combination of active and inactive RAS-binding compounds. Proc Natl Acad Sci U S A. 2019 Feb 12;116(7):2545-2550.
REF 8 BRET-based RAS biosensors that show a novel small molecule is an inhibitor of RAS-effector protein-protein interactions. Elife. 2018 Jul 10;7:e37122.
REF 9 KRAS interaction with RAF1 RAS-binding domain and cysteine-rich domain provides insights into RAS-mediated RAF activation. Nat Commun. 2021 Feb 19;12(1):1176.
REF 10 Atypical KRAS(G12R) Mutant Is Impaired in PI3K Signaling and Macropinocytosis in Pancreatic Cancer. Cancer Discov. 2020 Jan;10(1):104-123.
REF 11 Exceptionally high-affinity Ras binders that remodel its effector domain. J Biol Chem. 2018 Mar 2;293(9):3265-3280.
REF 12 KRAS G13D sensitivity to neurofibromin-mediated GTP hydrolysis. Proc Natl Acad Sci U S A. 2019 Oct 29;116(44):22122-22131.
REF 13 RAS interaction with Sin1 is dispensable for mTORC2 assembly and activity. Proc Natl Acad Sci U S A. 2021 Aug 17;118(33):e2103261118.
REF 14 Machine learning-driven multiscale modeling reveals lipid-dependent dynamics of RAS signaling proteins. Proc Natl Acad Sci U S A. 2022 Jan 4;119(1):e2113297119.
REF 15 Structural Insights into the SPRED1-Neurofibromin-KRAS Complex and Disruption of SPRED1-Neurofibromin Interaction by Oncogenic EGFR. Cell Rep. 2020 Jul 21;32(3):107909.
REF 16 GTP-State-Selective Cyclic Peptide Ligands of K-Ras(G12D) Block Its Interaction with Raf. ACS Cent Sci. 2020 Oct 28;6(10):1753-1761.
REF 17 GTP hydrolysis is modulated by Arg34 in the RASopathy-associated KRAS(P34R). Birth Defects Res. 2020 Jun;112(10):708-717.
REF 18 Structures of N-terminally processed KRAS provide insight into the role of N-acetylation. Sci Rep. 2019 Jul 19;9(1):10512.
REF 19 An engineered protein antagonist of K-Ras/B-Raf interaction. Sci Rep. 2017 Jul 19;7(1):5831.
REF 20 Isoform-Specific Destabilization of the Active Site Reveals a Molecular Mechanism of Intrinsic Activation of KRas G13D. Cell Rep. 2019 Aug 6;28(6):1538-1550.e7.

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