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 Guanosine 5'-triphosphate P3-[1-(2-nitrophenyl)ethyl ester] Ligand Info
Canonical SMILES CC(C1=CC=CC=C1[N+](=O)[O-])OP(=O)(O)OP(=O)(O)OP(=O)(O)OCC2C(C(C(O2)N3C=NC4=C3N=C(NC4=O)N)O)O
InChI 1S/C18H23N6O16P3/c1-8(9-4-2-3-5-10(9)24(28)29)38-42(32,33)40-43(34,35)39-41(30,31)36-6-11-13(25)14(26)17(37-11)23-7-20-12-15(23)21-18(19)22-16(12)27/h2-5,7-8,11,13-14,17,25-26H,6H2,1H3,(H,30,31)(H,32,33)(H,34,35)(H3,19,21,22,27)/t8-,11-,13-,14-,17-/m1/s1
InChIKey NYWDUFBXCCSYMK-JPDTYCKISA-N
PubChem Compound ID 135509080
Drug Binding Sites of Target  Top
PDB ID: 2EVW      Crystal structure analysis of a fluorescent form of H-Ras p21 in complex with R-caged GTP
Method X-ray diffraction Resolution 1.05 Å Mutation Yes [1]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
ECDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHQYREQI
100

KRVKDSDDVP
110
MVLVGNKSDL
120
AARTVESRQA
130
QDLARSYGIP
140
YIETSAKTRQ
150

GVEDAFYTLV
160
REIRQH
Residue
Distance (Å)
ALA11
3.792
GLY12
2.753
GLY13
2.925
VAL14
3.291
GLY15
3.060
LYS16
2.572
SER17
2.976
ALA18
2.708
LEU19
4.694
PHE28
3.459
VAL29
2.954
ASP30
3.676
GLU31
3.486
CYS32
3.819
ASP33
4.553
Residue
Distance (Å)
PRO34
3.889
THR35
3.026
ASP57
4.532
THR58
4.184
ALA59
4.748
GLY60
3.819
ASN116
2.969
LYS117
3.274
SER118
4.630
ASP119
2.657
LEU120
3.542
THR144
4.721
SER145
3.358
ALA146
2.732
LYS147
3.668
PDB ID: 2CL6      CRYSTAL STRUCTURE ANALYSIS OF A FLUORESCENT FORM OF H-RAS P21 IN COMPLEX WITH S-caged GTP
Method X-ray diffraction Resolution 1.24 Å Mutation Yes [1]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
ECDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHQYREQI
100

KRVKDSDDVP
110
MVLVGNKSDL
120
AARTVESRQA
130
QDLARSYGIP
140
YIETSAKTRQ
150

GVEDAFYTLV
160
REIRQH
Residue
Distance (Å)
GLY10
4.922
ALA11
3.652
GLY12
3.845
GLY13
3.119
VAL14
3.403
GLY15
3.059
LYS16
2.562
SER17
2.821
ALA18
2.730
LEU19
4.796
PHE28
3.399
VAL29
2.338
ASP30
2.528
GLU31
3.924
CYS32
3.045
ASP33
2.831
Residue
Distance (Å)
PRO34
3.609
ASP57
4.686
THR58
4.627
ALA59
3.847
GLY60
2.697
GLN61
2.713
ASN116
3.157
LYS117
3.140
SER118
4.755
ASP119
2.853
LEU120
3.427
THR144
4.447
SER145
3.409
ALA146
2.883
LYS147
3.707
PDB ID: 1GNR      X-RAY CRYSTAL STRUCTURE ANALYSIS OF THE CATALYTIC DOMAIN OF THE ONCOGENE PRODUCT P21H-RAS COMPLEXED WITH CAGED GTP AND MANT DGPPNHP
Method X-ray diffraction Resolution 1.85 Å Mutation No [2]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHQYREQI
100

KRVKDSDDVP
110
MVLVGNKCDL
120
AARTVESRQA
130
QDLARSYGIP
140
YIETSAKTRQ
150

GVEDAFYTLV
160
REIRQH
Residue
Distance (Å)
ALA11
4.051
GLY12
3.041
GLY13
3.110
VAL14
3.274
GLY15
3.070
LYS16
2.812
SER17
3.138
ALA18
2.760
PHE28
2.938
VAL29
2.874
ASP30
3.335
GLU31
4.650
TYR32
2.898
THR35
2.809
Residue
Distance (Å)
ASP57
4.741
THR58
4.239
ALA59
4.635
GLY60
3.556
GLN61
4.976
ASN116
3.361
LYS117
2.620
CYS118
4.836
ASP119
2.939
LEU120
3.744
THR144
4.649
SER145
3.424
ALA146
2.914
LYS147
3.540
PDB ID: 1GNQ      X-RAY CRYSTAL STRUCTURE ANALYSIS OF THE CATALYTIC DOMAIN OF THE ONCOGENE PRODUCT P21H-RAS COMPLEXED WITH CAGED GTP AND MANT DGPPNHP
Method X-ray diffraction Resolution 2.50 Å Mutation No [2]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHQYREQI
100

KRVKDSDDVP
110
MVLVGNKCDL
120
AARTVESRQA
130
QDLARSYGIP
140
YIETSAKTRQ
150

GVEDAFYTLV
160
REIRQH
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CAG or .CAG2 or .CAG3 or :3CAG;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:32 or .A:33 or .A:34 or .A:35 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
4.081
GLY12
3.488
GLY13
2.727
VAL14
3.479
GLY15
2.837
LYS16
2.871
SER17
3.180
ALA18
3.230
PHE28
2.927
VAL29
3.390
ASP30
3.628
TYR32
4.286
ASP33
3.950
PRO34
3.239
Residue
Distance (Å)
THR35
3.948
THR58
4.197
ALA59
4.131
GLY60
2.908
GLN61
4.153
ASN116
3.195
LYS117
2.601
CYS118
4.924
ASP119
3.197
LEU120
3.832
THR144
4.675
SER145
3.410
ALA146
2.893
LYS147
3.921
PDB ID: 1PLJ      CRYSTALLOGRAPHIC STUDIES ON P21H-RAS USING SYNCHROTRON LAUE METHOD: IMPROVEMENT OF CRYSTAL QUALITY AND MONITORING OF THE GTPASE REACTION AT DIFFERENT TIME POINTS
Method X-ray diffraction Resolution 2.80 Å Mutation No [3]
PDB Sequence
MTEYKLVVVG
10
APGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVIDGETC
51

LLDIDTAGSA
66
MDQYMTGGFL
79
CFAINNTSED
92
IHQYREQIKR
102
VKDSDDVPMV
112

LVGNKCDLAA
122
RVESRQAQDL
133
ARSYGIPYIE
143
TSAKTRQGVE
153
DAFYTLVREI
163

QH
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CAG or .CAG2 or .CAG3 or :3CAG;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: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 #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ALA11
4.194
PRO12
3.306
GLY13
3.772
VAL14
3.598
GLY15
2.781
LYS16
2.594
SER17
3.024
ALA18
2.984
PHE28
2.991
VAL29
2.979
ASP30
3.538
GLU31
4.991
TYR32
2.827
ASP33
4.874
Residue
Distance (Å)
THR35
2.862
ASP57
4.296
THR58
4.391
ALA59
4.231
GLY60
3.278
ASN116
3.544
LYS117
2.589
ASP119
3.201
LEU120
3.581
THR144
4.636
SER145
3.467
ALA146
3.395
LYS147
4.150
References  Top
REF 1 A newly designed microspectrofluorometer for kinetic studies on protein crystals in combination with x-ray diffraction. Biophys J. 2006 Aug 1;91(3):981-92.
REF 2 X-ray crystal structure analysis of the catalytic domain of the oncogene product p21H-ras complexed with caged GTP and mant dGppNHp. J Mol Biol. 1995 Oct 13;253(1):132-50.
REF 3 Crystallographic studies on p21(H-ras) using the synchrotron Laue method: improvement of crystal quality and monitoring of the GTPase reaction at different time points. Acta Crystallogr D Biol Crystallogr. 1994 Jul 1;50(Pt 4):512-20.

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