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 T71081 Target Info
Target Name GTPase HRas (HRAS)
Synonyms p21ras; cHras; c-H-ras; Transforming protein p21; HaRas; Ha-Ras; H-Ras-1; GTPase HRas, Nterminally processed
Target Type Literature-reported Target
Gene Name HRAS
Biochemical Class Small GTPase
UniProt ID
RASH_HUMAN
Ligand General Information  Top
Ligand Name Dithioerythritol Ligand Info
Canonical SMILES C(C(C(CS)O)O)S
InChI 1S/C4H10O2S2/c5-3(1-7)4(6)2-8/h3-8H,1-2H2/t3-,4+
InChIKey VHJLVAABSRFDPM-ZXZARUISSA-N
PubChem Compound ID 439352
Drug Binding Sites of Target  Top
PDB ID: 4DLR      H-Ras PEG 400/Ca(OAc)2, ordered off
Method X-ray diffraction Resolution 1.32 Å Mutation No [1]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEYSAMRDE
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHQYREQI
100

KRVKDSDDVP
110
MVLVGNKCDL
120
AARTVESRQA
130
QDLARSYGIP
140
YIETSAKTRQ
150

GVEDAFYTLV
160
REIRQH
Residue
Distance (Å)
ARG68
3.233
LYS88
4.801
ASP92
3.590
GLN95
3.166
Residue
Distance (Å)
TYR96
2.736
GLN99
3.743
ARG102
4.793
PDB ID: 4DLZ      H-Ras Set 2 Ca(OAc)2/DTE, ordered off
Method X-ray diffraction Resolution 1.66 Å Mutation No [1]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEYSAMRDE
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHQYREQI
100

KRVKDSDDVP
110
MVLVGNKCDL
120
AARTVESRQA
130
QDLARSYGIP
140
YIETSAKTRQ
150

GVEDAFYTLV
160
REIRQH
Residue
Distance (Å)
TYR32
3.290
PRO34
3.199
GLN61
3.727
TYR64
3.788
ARG68
3.260
Residue
Distance (Å)
ASP92
3.915
GLN95
3.053
TYR96
3.269
GLN99
3.844
ARG102
4.163
PDB ID: 4DLX      H-Ras Set 1 CaCl2/DTE, ordered off
Method X-ray diffraction Resolution 1.73 Å Mutation No [1]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEYSAMRDE
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHQYREQI
100

KRVKDSDDVP
110
MVLVGNKCDL
120
AARTVESRQA
130
QDLARSYGIP
140
YIETSAKTRQ
150

GVEDAFYTLV
160
REIRQH
Residue
Distance (Å)
ARG68
3.098
ASP92
3.368
GLN95
2.633
Residue
Distance (Å)
TYR96
3.482
GLN99
3.871
PDB ID: 4G0N      Crystal Structure of wt H-Ras-GppNHp bound to the RBD of Raf Kinase
Method X-ray diffraction Resolution 2.45 Å Mutation No [2]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEAMRDQYM
72
RTGEGFLCVF
82
AINNTKSFED
92
IHQYREQIKR
102

VKDSDDVPMV
112
LVGNKCDLAA
122
RTVESRQAQD
132
LARSYGIPYI
142
ETSAKTRQGV
152

EDAFYTLVRE
162
IRQH
Click to Show 3D Structure of This Binding Site
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Residue
Distance (Å)
ARG68
3.319
LYS88
4.631
ASP92
3.558
Residue
Distance (Å)
GLN95
3.309
TYR96
3.338
GLN99
3.288
References  Top
REF 1 Shift in the equilibrium between on and off states of the allosteric switch in Ras-GppNHp affected by small molecules and bulk solvent composition. Biochemistry. 2012 Aug 7;51(31):6114-26.
REF 2 Allosteric effects of the oncogenic RasQ61L mutant on Raf-RBD. Structure. 2015 Mar 3;23(3):505-516.

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