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 T50594 Target Info
Target Name Serine/threonine-protein kinase pim-1 (PIM1)
Synonyms Pim-1 proto-oncogene, serine/threonine kinase; PIM
Target Type Clinical trial Target
Gene Name PIM1
Biochemical Class Kinase
UniProt ID
PIM1_HUMAN
Ligand General Information  Top
Ligand Name AMP-PNP Ligand Info
Canonical SMILES C1=NC(=C2C(=N1)N(C=N2)C3C(C(C(O3)COP(=O)(O)OP(=O)(NP(=O)(O)O)O)O)O)N
InChI 1S/C10H17N6O12P3/c11-8-5-9(13-2-12-8)16(3-14-5)10-7(18)6(17)4(27-10)1-26-31(24,25)28-30(22,23)15-29(19,20)21/h2-4,6-7,10,17-18H,1H2,(H,24,25)(H2,11,12,13)(H4,15,19,20,21,22,23)/t4-,6-,7-,10-/m1/s1
InChIKey PVKSNHVPLWYQGJ-KQYNXXCUSA-N
PubChem Compound ID 33113
Drug Binding Sites of Target  Top
PDB ID: 2BZK      CRYSTAL STRUCTURE OF THE HUMAN PIM1 IN COMPLEX WITH AMPPNP AND PIMTIDE
Method X-ray diffraction Resolution 2.45 Å Mutation Yes [1]
PDB Sequence
PLESQYQVGP
42
LLGSVYSGIR
57
VSDNLPVAIK
67
HVEKDRISDW
77
GELPNGTRVP
87

MEVVLLKKVS
97
SGFSGVIRLL
107
DWFERPDSFV
117
LILERPEPVQ
127
DLFDFITERG
137

ALQEELARSF
147
FWQVLEAVRH
157
CHNCGVLHRD
167
IKDENILIDL
177
NRGELKLIDF
187

GSGALLKDTV
197
YTDFDGTRVY
207
SPPEWIRYHR
217
YHGRSAAVWS
227
LGILLYDMVC
237

GDIPFEHDEE
247
IIGGQVFFRQ
257
RVSSECQHLI
267
RWCLALRPSD
277
RPTFEEIQNH
287

PWMQDVLLPQ
297
ETAEIHLH
Residue
Distance (Å)
LEU44
3.800
GLY45
4.151
SER51
2.751
VAL52
3.777
ALA65
3.670
LYS67
2.670
HIS68
3.638
VAL69
4.697
GLU89
4.783
ILE104
4.233
LEU120
3.796
Residue
Distance (Å)
GLU121
2.673
ARG122
3.802
PRO123
4.173
VAL126
4.826
ASP128
3.639
GLU171
4.186
ASN172
3.900
LEU174
3.719
ILE185
3.844
ASP186
2.748
PDB ID: 3A99      Structure of PIM-1 kinase crystallized in the presence of P27KIP1 Carboxy-terminal peptide
Method X-ray diffraction Resolution 1.60 Å Mutation No [2]
PDB Sequence
PLESQYQVGP
42
LLGSGGFGSV
52
YSGIRVSDNL
62
PVAIKHVEKD
72
RISDWGELPN
82

GTRVPMEVVL
92
LKKVSSGFSG
102
VIRLLDWFER
112
PDSFVLILER
122
PEPVQDLFDF
132

ITERGALQEE
142
LARSFFWQVL
152
EAVRHCHNCG
162
VLHRDIKDEN
172
ILIDLNRGEL
182

KLIDFGSGAL
192
LKDTVYTDFD
202
GTRVYSPPEW
212
IRYHRYHGRS
222
AAVWSLGILL
232

YDMVCGDIPF
242
EHDEEIIRGQ
252
VFFRQRVSSE
262
CQHLIRWCLA
272
LRPSDRPTFE
282

EIQNHPWMQD
292
VLLPQETAEI
302
HLH
Residue
Distance (Å)
LEU44
3.611
GLY45
3.770
GLY47
4.227
GLY48
4.034
PHE49
4.480
GLY50
3.536
SER51
4.783
VAL52
3.487
ALA65
3.475
LYS67
2.786
GLU89
4.989
ILE104
3.568
Residue
Distance (Å)
LEU120
3.932
GLU121
2.741
ARG122
3.833
PRO123
4.004
VAL126
4.522
ASP128
4.306
GLU171
4.547
ASN172
4.020
LEU174
3.538
ILE185
3.926
ASP186
3.021
PDB ID: 1XR1      Crystal structure of hPim-1 kinase in complex with AMP-PNP at 2.1 A Resolution
Method X-ray diffraction Resolution 2.10 Å Mutation No [3]
PDB Sequence
EPLESQYQVG
41
PLLGSGGFGS
51
VYSGIRVSDN
61
LPVAIKHVEK
71
DRISDWGELP
81

NGTRVPMEVV
91
LLKKVSSGFS
101
GVIRLLDWFE
111
RPDSFVLILE
121
RPEPVQDLFD
131

FITERGALQE
141
ELARSFFWQV
151
LEAVRHCHNC
161
GVLHRDIKDE
171
NILIDLNRGE
181

LKLIDFGSGA
191
LLKDTVYTDF
201
DGTRVYSPPE
211
WIRYHRYHGR
221
SAAVWSLGIL
231

LYDMVCGDIP
241
FEHDEEIIRG
251
QVFFRQRVSS
261
ECQHLIRWCL
271
ALRPSDRPTF
281

EEIQNHPWMQ
291
DVLLPQETAE
301
IHLHSLS
Residue
Distance (Å)
LEU44
3.705
GLY45
4.112
GLY47
4.346
PHE49
3.860
GLY50
3.429
SER51
4.516
VAL52
3.011
ALA65
3.555
LYS67
3.066
ARG73
3.804
ILE104
3.900
Residue
Distance (Å)
LEU120
3.911
GLU121
2.935
ARG122
3.420
PRO123
4.005
VAL126
4.382
ASP128
4.343
GLU171
4.438
ASN172
3.909
LEU174
3.522
ILE185
3.898
ASP186
3.081
PDB ID: 1YXT      Crystal Structure of Kinase Pim1 in complex with AMPPNP
Method X-ray diffraction Resolution 2.00 Å Mutation No [4]
PDB Sequence
PLESQYQVGP
42
LLGSGGFGSV
52
YSGIRVSDNL
62
PVAIKHVEKD
72
RISDWGELPN
82

GTRVPMEVVL
92
LKKVSSGFSG
102
VIRLLDWFER
112
PDSFVLILER
122
PEPVQDLFDF
132

ITERGALQEE
142
LARSFFWQVL
152
EAVRHCHNCG
162
VLHRDIKDEN
172
ILIDLNRGEL
182

KLIDFGSGAL
192
LKDTVYTDFD
202
GTRVYSPPEW
212
IRYHRYHGRS
222
AAVWSLGILL
232

YDMVCGDIPF
242
EHDEEIIRGQ
252
VFFRQRVSSE
262
CQHLIRWCLA
272
LRPSDRPTFE
282

EIQNHPWMQD
292
VLLPQETAEI
302
HLHS
Click to Show 3D Structure of This Binding Site
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Residue
Distance (Å)
LEU44
3.666
GLY45
3.974
SER46
3.650
GLY47
4.324
GLY48
3.255
PHE49
2.813
GLY50
2.729
VAL52
3.351
ALA65
3.331
LYS67
2.694
GLU89
4.656
ILE104
3.672
LEU120
3.914
Residue
Distance (Å)
GLU121
2.873
ARG122
3.708
PRO123
4.098
VAL126
4.069
ASP128
2.856
ASP167
3.550
LYS169
4.186
GLU171
2.792
ASN172
2.082
LEU174
3.407
ILE185
3.581
ASP186
1.607
References  Top
REF 1 Crystal Structure of the Human Pim1 in Complex with Amppnp and Pimtide
REF 2 Cell-permeable carboxyl-terminal p27(Kip1) peptide exhibits anti-tumor activity by inhibiting Pim-1 kinase. J Biol Chem. 2011 Jan 28;286(4):2681-8.
REF 3 Structural basis of constitutive activity and a unique nucleotide binding mode of human Pim-1 kinase. J Biol Chem. 2005 Feb 18;280(7):6130-7.
REF 4 Crystal structures of proto-oncogene kinase Pim1: a target of aberrant somatic hypermutations in diffuse large cell lymphoma. J Mol Biol. 2005 Apr 22;348(1):183-93.

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