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 Phosphomethylphosphonic Acid Guanylate Ester Ligand Info
Canonical SMILES C1=NC2=C(N1C3C(C(C(O3)COP(=O)(CP(=O)(O)OP(=O)(O)O)O)O)O)N=C(NC2=O)N
InChI 1S/C11H18N5O13P3/c12-11-14-8-5(9(19)15-11)13-2-16(8)10-7(18)6(17)4(28-10)1-27-30(20,21)3-31(22,23)29-32(24,25)26/h2,4,6-7,10,17-18H,1,3H2,(H,20,21)(H,22,23)(H2,24,25,26)(H3,12,14,15,19)/t4-,6-,7-,10-/m1/s1
InChIKey GXTIEXDFEKYVGY-KQYNXXCUSA-N
PubChem Compound ID 135440070
Drug Binding Sites of Target  Top
PDB ID: 6Q21      MOLECULAR SWITCH FOR SIGNAL TRANSDUCTION: STRUCTURAL DIFFERENCES BETWEEN ACTIVE AND INACTIVE FORMS OF PROTOONCOGENIC RAS PROTEINS
Method X-ray diffraction Resolution 1.95 Å Mutation No [1]
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
REIRQHKLRK
170
L
Residue
Distance (Å)
ALA11
3.725
GLY12
3.423
GLY13
3.455
VAL14
3.191
GLY15
2.792
LYS16
2.257
SER17
3.148
ALA18
3.094
PHE28
3.493
VAL29
3.943
ASP30
2.716
GLU31
4.855
TYR32
3.888
ASP33
4.889
Residue
Distance (Å)
PRO34
3.691
THR35
2.660
THR58
4.010
ALA59
3.328
GLY60
3.136
GLN61
3.155
ASN116
2.963
LYS117
3.298
ASP119
2.806
LEU120
4.399
THR144
4.353
SER145
3.243
ALA146
2.575
LYS147
3.320
PDB ID: 6ZJ0      CRYSTAL STRUCTURE OF HRAS-G12D IN COMPLEX WITH GCP AND COMPOUND 18
Method X-ray diffraction Resolution 1.76 Å Mutation No [2]
PDB Sequence
MTEYKLVVVG
10
ADGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QAMRDQYMRT
74
GEGFLCVFAI
84
NNTKSFEDIH
94
QYREQIKRVK
104

DSDDVPMVLV
114
GNKCDLAART
124
VESRQAQDLA
134
RSYGIPYIET
144
SAKTRQGVED
154

AFYTLVREIR
164
QH
Residue
Distance (Å)
ALA11
3.899
ASP12
2.481
GLY13
1.893
VAL14
2.904
GLY15
2.210
LYS16
1.730
SER17
1.907
ALA18
1.818
LEU19
4.446
PHE28
2.774
VAL29
1.966
ASP30
2.579
GLU31
2.923
TYR32
2.492
ASP33
3.793
PRO34
2.525
Residue
Distance (Å)
THR35
2.234
ASP57
4.664
THR58
4.014
ALA59
3.447
GLY60
2.378
GLN61
4.932
ASN116
2.463
LYS117
2.431
CYS118
4.553
ASP119
1.860
LEU120
2.471
THR144
4.698
SER145
2.615
ALA146
2.196
LYS147
2.533
THR148
4.895
PDB ID: 121P      STRUKTUR UND GUANOSINTRIPHOSPHAT-HYDROLYSEMECHANISMUS DES C-TERMINAL VERKUERZTEN MENSCHLICHEN KREBSPROTEINS P21-H-RAS
Method X-ray diffraction Resolution 1.54 Å Mutation No [3]
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
3.943
GLY12
3.542
GLY13
3.421
VAL14
3.139
GLY15
2.971
LYS16
2.725
SER17
2.915
ALA18
2.772
PHE28
3.232
VAL29
2.579
ASP30
3.371
GLU31
4.125
ASP33
4.417
PRO34
3.489
THR35
3.103
Residue
Distance (Å)
ASP57
4.873
THR58
3.821
ALA59
4.027
GLY60
2.953
GLN61
4.920
ASN116
3.153
LYS117
3.077
CYS118
4.851
ASP119
2.818
LEU120
3.520
THR144
4.518
SER145
3.473
ALA146
2.820
LYS147
3.576
PDB ID: 1JAH      H-RAS P21 PROTEIN MUTANT G12P, COMPLEXED WITH GUANOSINE-5'-[BETA,GAMMA-METHYLENE] TRIPHOSPHATE AND MAGNESIUM
Method X-ray diffraction Resolution 1.80 Å Mutation Yes [4]
PDB Sequence
MTEYKLVVVG
10
APGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHQYREQI
100

KRVKDSDDVP
110
MVLVGNKCDL
120
AGRTVESRQA
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 .GCP or .GCP2 or .GCP3 or :3GCP;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: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
4.012
PRO12
3.283
GLY13
3.321
VAL14
3.165
GLY15
3.012
LYS16
2.757
SER17
2.987
ALA18
2.728
PHE28
3.119
VAL29
2.642
ASP30
3.164
GLU31
3.784
TYR32
4.978
ASP33
4.415
PRO34
3.550
Residue
Distance (Å)
THR35
3.159
ASP57
4.919
THR58
4.017
ALA59
4.695
GLY60
4.158
ASN116
3.297
LYS117
3.147
CYS118
4.827
ASP119
3.018
LEU120
3.798
THR144
4.755
SER145
3.463
ALA146
2.813
LYS147
3.574
PDB ID: 1JAI      H-RAS P21 PROTEIN MUTANT G12P, COMPLEXED WITH GUANOSINE-5'-[BETA,GAMMA-METHYLENE] TRIPHOSPHATE AND MANGANESE
Method X-ray diffraction Resolution 1.80 Å Mutation Yes [4]
PDB Sequence
MTEYKLVVVG
10
APGVGKSALT
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 .GCP or .GCP2 or .GCP3 or :3GCP;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: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
4.074
PRO12
3.223
GLY13
3.238
VAL14
3.172
GLY15
3.031
LYS16
2.790
SER17
2.941
ALA18
2.672
PHE28
3.245
VAL29
2.699
ASP30
3.129
GLU31
3.968
TYR32
4.822
ASP33
4.461
PRO34
3.601
Residue
Distance (Å)
THR35
3.241
ASP57
4.974
THR58
4.170
ALA59
4.759
GLY60
3.793
ASN116
3.330
LYS117
3.077
CYS118
4.835
ASP119
2.859
LEU120
3.699
THR144
4.728
SER145
3.453
ALA146
2.936
LYS147
3.462
References  Top
REF 1 Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins. Science. 1990 Feb 23;247(4945):939-45.
REF 2 Drugging all RAS isoforms with one pocket. Future Med Chem. 2020 Nov;12(21):1911-1923.
REF 3 Struktur Und Guanosintriphosphat-Hydrolysemechanismus Des C-Terminal Verkuerzten Menschlichen Krebsproteins P21-H-Ras
REF 4 The role of the metal ion in the p21ras catalysed GTP-hydrolysis: Mn2+ versus Mg2+. J Mol Biol. 1997 Mar 7;266(4):847-56.

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