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'-Diphosphate Ligand Info
Canonical SMILES C1=NC2=C(N1C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N=C(NC2=O)N
InChI 1S/C10H15N5O11P2/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(25-9)1-24-28(22,23)26-27(19,20)21/h2-3,5-6,9,16-17H,1H2,(H,22,23)(H2,19,20,21)(H3,11,13,14,18)/t3-,5-,6-,9-/m1/s1
InChIKey QGWNDRXFNXRZMB-UUOKFMHZSA-N
PubChem Compound ID 135398619
Drug Binding Sites of Target  Top
PDB ID: 4Q21      MOLECULAR SWITCH FOR SIGNAL TRANSDUCTION: STRUCTURAL DIFFERENCES BETWEEN ACTIVE AND INACTIVE FORMS OF PROTOONCOGENIC RAS PROTEINS
Method X-ray diffraction Resolution 2.00 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
REIRQHKLR
Residue
Distance (Å)
ALA11
4.301
GLY12
3.629
GLY13
2.668
VAL14
3.710
GLY15
3.127
LYS16
2.489
SER17
2.866
ALA18
2.819
PHE28
3.198
VAL29
4.414
ASP30
2.960
GLU31
4.706
Residue
Distance (Å)
TYR32
3.861
PRO34
4.894
ASP57
4.821
ASN116
3.290
LYS117
2.823
ASP119
2.572
LEU120
2.787
THR144
4.819
SER145
3.468
ALA146
2.740
LYS147
3.329
PDB ID: 1AA9      HUMAN C-HA-RAS(1-171)(DOT)GDP, NMR, MINIMIZED AVERAGE STRUCTURE
Method Solution NMR Resolution N.A. 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
REIRQHKLRK
170
L
Residue
Distance (Å)
ALA11
4.224
GLY12
2.377
GLY13
2.785
VAL14
4.032
GLY15
2.073
LYS16
2.069
SER17
2.093
ALA18
2.793
LEU19
4.922
PHE28
2.101
ASP30
2.010
GLU31
4.722
TYR32
3.506
Residue
Distance (Å)
ASP33
4.166
PRO34
3.775
VAL81
4.620
ASN116
3.952
LYS117
2.292
CYS118
4.873
ASP119
2.969
LEU120
4.304
THR144
4.774
SER145
2.368
ALA146
2.268
LYS147
2.060
THR148
3.857
PDB ID: 5VBE      Crystal Structure of Small Molecule Disulfide 2C07 Bound to H-Ras M72C GDP
Method X-ray diffraction Resolution 1.57 Å Mutation Yes [3]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QSAMRDQYCR
73
TGEGFLCVFA
83
INNTKSFEDI
93
HQYREQIKRV
103

KDSDDVPMVL
113
VGNKCDLAAR
123
TVESRQAQDL
133
ARSYGIPYIE
143
TSAKTRQGVE
153

DAFYTLVREI
163
RQH
Residue
Distance (Å)
ALA11
3.799
GLY12
3.175
GLY13
1.923
VAL14
2.874
GLY15
2.267
LYS16
1.963
SER17
2.152
ALA18
1.959
LEU19
4.520
PHE28
2.318
VAL29
2.305
ASP30
2.588
GLU31
3.371
Residue
Distance (Å)
TYR32
3.431
PRO34
4.410
ASP57
4.800
ASN116
2.406
LYS117
2.531
CYS118
4.526
ASP119
1.829
LEU120
2.272
THR144
4.670
SER145
2.705
ALA146
2.238
LYS147
2.856
PDB ID: 4L9S      Crystal Structure of H-Ras G12C, GDP-bound
Method X-ray diffraction Resolution 1.61 Å Mutation Yes [4]
PDB Sequence
MTEYKLVVVG
10
ACGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
RDQYMRTGEG
77
FLCVFAINNT
87
KSFEDIHQYR
97
EQIKRVKDSD
107

DVPMVLVGNK
117
CDLAARTVES
127
RQAQDLARSY
137
GIPYIETSAK
147
TRQGVEDAFY
157

TLVREIRQH
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GDP or .GDP2 or .GDP3 or :3GDP;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: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
3.800
CYS12
3.145
GLY13
1.905
VAL14
2.909
GLY15
2.282
LYS16
1.994
SER17
2.216
ALA18
2.011
LEU19
4.588
PHE28
2.791
VAL29
2.383
ASP30
1.928
GLU31
3.688
Residue
Distance (Å)
TYR32
3.632
PRO34
4.218
ASP57
4.638
ASN116
2.419
LYS117
2.514
CYS118
4.490
ASP119
1.907
LEU120
2.464
THR144
4.621
SER145
2.666
ALA146
2.269
LYS147
2.772
PDB ID: 1IOZ      Crystal Structure of the C-HA-RAS Protein Prepared by the Cell-Free Synthesis
Method X-ray diffraction Resolution 2.00 Å Mutation No [5]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
RDQYMRTGEG
77
FLCVFAINNT
87
KSFEDIHQYR
97
EQIKRVKDSD
107

DVPMVLVGNK
117
CDLAARTVES
127
RQAQDLARSY
137
GIPYIETSAK
147
TRQGVEDAFY
157

TLVREIRQHK
167
LR
Click to Show 3D Structure of This Binding Site
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Residue
Distance (Å)
ALA11
3.828
GLY12
3.812
GLY13
2.814
VAL14
3.390
GLY15
2.933
LYS16
2.688
SER17
3.038
ALA18
2.790
LEU19
4.950
PHE28
3.196
VAL29
4.255
ASP30
3.057
Residue
Distance (Å)
GLU31
4.145
TYR32
4.044
ASP57
4.790
ASN116
3.177
LYS117
3.127
CYS118
4.947
ASP119
2.841
LEU120
3.368
THR144
4.744
SER145
3.402
ALA146
2.835
LYS147
3.401
PDB ID: 1Q21      CRYSTAL STRUCTURES AT 2.2 ANGSTROMS RESOLUTION OF THE CATALYTIC DOMAINS OF NORMAL RAS PROTEIN AND AN ONCOGENIC MUTANT COMPLEXED WITH GSP
Method X-ray diffraction Resolution 2.20 Å Mutation No [6]
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
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set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GDP or .GDP2 or .GDP3 or :3GDP;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:57 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
3.816
GLY12
3.566
GLY13
2.756
VAL14
3.239
GLY15
2.735
LYS16
2.766
SER17
3.051
ALA18
2.852
PHE28
3.117
VAL29
3.575
ASP30
3.169
Residue
Distance (Å)
GLU31
4.075
TYR32
3.795
ASP57
4.795
ASN116
3.002
LYS117
2.689
ASP119
2.743
LEU120
3.775
THR144
4.719
SER145
3.333
ALA146
2.581
LYS147
3.286
PDB ID: 2Q21      CRYSTAL STRUCTURES AT 2.2 ANGSTROMS RESOLUTION OF THE CATALYTIC DOMAINS OF NORMAL RAS PROTEIN AND AN ONCOGENIC MUTANT COMPLEXED WITH GSP
Method X-ray diffraction Resolution 2.20 Å Mutation Yes [6]
PDB Sequence
MTEYKLVVVG
10
AVGVGKSALT
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
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GDP or .GDP2 or .GDP3 or :3GDP;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:57 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
3.860
VAL12
3.559
GLY13
2.628
VAL14
3.063
GLY15
2.886
LYS16
2.674
SER17
2.937
ALA18
2.704
LEU19
4.992
PHE28
3.075
VAL29
3.380
ASP30
3.381
Residue
Distance (Å)
GLU31
4.326
TYR32
3.785
ASP57
4.957
ASN116
2.995
LYS117
2.409
CYS118
4.971
ASP119
2.755
LEU120
3.689
THR144
4.805
SER145
3.338
ALA146
2.751
LYS147
3.441
PDB ID: 5E95      Crystal Structure of Mb(NS1)/H-Ras Complex
Method X-ray diffraction Resolution 1.40 Å Mutation No [7]
PDB Sequence
GSMTEYKLVV
8
VGAGGVGKSA
18
LTIQLIQNHF
28
VDEYDPTIED
38
SYRKQVVIDG
48

ETCLLDILDT
58
AGQEEYSAMR
68
DQYMRTGEGF
78
LCVFAINNTK
88
SFEDIHQYRE
98

QIKRVKDSDD
108
VPMVLVGNKC
118
DLAARTVESR
128
QAQDLARSYG
138
IPYIETSAKT
148

RQGVEDAFYT
158
LVREIRQH
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set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GDP or .GDP2 or .GDP3 or :3GDP;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:57 or .A:59 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
3.752
GLY12
3.815
GLY13
2.813
VAL14
3.309
GLY15
3.082
LYS16
2.798
SER17
2.729
ALA18
2.727
LEU19
4.991
PHE28
3.284
VAL29
2.960
ASP30
2.667
Residue
Distance (Å)
ASP57
4.558
ALA59
3.536
ASN116
3.112
LYS117
3.106
CYS118
4.757
ASP119
2.799
LEU120
3.463
THR144
4.427
SER145
3.402
ALA146
2.803
LYS147
3.612
PDB ID: 6MQT      HRAS G12S in complex with GDP
Method X-ray diffraction Resolution 1.50 Å Mutation Yes [8]
PDB Sequence
AMTEYKLVVV
9
GASGVGKSAL
19
TIQLIQNHFV
29
DEYDPTIEDS
39
YRKQVVIDGE
49

TCLLDILDTA
59
GQEEYSAMRD
69
QYMRTGEGFL
79
CVFAINNTKS
89
FEDIHQYREQ
99

IKRVKDSDDV
109
PMVLVGNKCD
119
LAARTVESRQ
129
AQDLARSYGI
139
PYIETSAKTR
149

QGVEDAFYTL
159
VREIRQH
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set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GDP or .GDP2 or .GDP3 or :3GDP;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:57 or .A:58 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
3.064
SER12
3.109
GLY13
1.930
VAL14
1.927
GLY15
2.081
LYS16
1.941
SER17
2.051
ALA18
1.958
LEU19
4.511
PHE28
2.834
VAL29
1.835
ASP30
2.292
GLU31
3.320
TYR32
3.170
Residue
Distance (Å)
ASP33
4.688
PRO34
3.510
ASP57
3.708
THR58
4.291
ASN116
2.392
LYS117
2.541
CYS118
4.587
ASP119
1.797
LEU120
2.438
THR144
4.525
SER145
2.598
ALA146
2.277
LYS147
2.757
THR148
4.975
PDB ID: 6ZL3      CRYSTAL STRUCTURE OF HRAS IN COMPLEX WITH COMPOUND 18 and GDP
Method X-ray diffraction Resolution 2.03 Å Mutation No [9]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QSAMRDQYMR
73
TGEGFLCVFA
83
INNTKSFEDI
93
HQYREQIKRV
103

KDSDDVPMVL
113
VGNKCDLAAR
123
TVESRQAQDL
133
ARSYGIPYIE
143
TSAKTRQGVE
153

DAFYTLVREI
163
RQH
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set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GDP or .GDP2 or .GDP3 or :3GDP;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:34 or .A:57 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
3.800
GLY12
3.755
GLY13
2.777
VAL14
3.263
GLY15
3.024
LYS16
2.630
SER17
3.124
ALA18
2.834
PHE28
3.390
VAL29
4.310
ASP30
3.170
GLU31
4.931
Residue
Distance (Å)
TYR32
3.963
PRO34
4.602
ASP57
4.692
ASN116
3.252
LYS117
3.104
CYS118
4.797
ASP119
2.713
LEU120
3.513
THR144
4.611
SER145
3.356
ALA146
2.855
LYS147
3.461
PDB ID: 1CRP      THE SOLUTION STRUCTURE AND DYNAMICS OF RAS P21. GDP DETERMINED BY HETERONUCLEAR THREE AND FOUR DIMENSIONAL NMR SPECTROSCOPY
Method Solution NMR Resolution N.A. Mutation No [10]
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
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set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GDP or .GDP2 or .GDP3 or :3GDP;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: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
2.951
GLY12
2.856
GLY13
1.995
VAL14
2.204
GLY15
1.992
LYS16
2.208
SER17
2.207
ALA18
2.369
LEU19
4.887
PHE28
3.081
VAL29
3.655
ASP30
2.567
GLU31
4.780
Residue
Distance (Å)
TYR32
3.690
PRO34
4.432
ASP57
4.443
ASN116
2.422
LYS117
3.383
CYS118
4.860
ASP119
2.220
LEU120
3.523
THR144
4.752
SER145
2.418
ALA146
2.232
LYS147
2.266
THR148
4.542
PDB ID: 1CRQ      THE SOLUTION STRUCTURE AND DYNAMICS OF RAS P21. GDP DETERMINED BY HETERONUCLEAR THREE AND FOUR DIMENSIONAL NMR SPECTROSCOPY
Method Solution NMR Resolution N.A. Mutation No [10]
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 .GDP or .GDP2 or .GDP3 or :3GDP;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:116 or .A:117 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
4.446
GLY12
3.330
GLY13
2.228
VAL14
3.855
GLY15
2.216
LYS16
2.222
SER17
2.595
ALA18
2.387
LEU19
4.725
PHE28
2.925
VAL29
4.301
Residue
Distance (Å)
ASP30
2.611
GLU31
3.621
TYR32
3.071
PRO34
4.726
ASN116
3.679
LYS117
3.136
ASP119
2.352
LEU120
3.681
SER145
2.902
ALA146
2.239
LYS147
2.116
PDB ID: 1CRR      THE SOLUTION STRUCTURE AND DYNAMICS OF RAS P21. GDP DETERMINED BY HETERONUCLEAR THREE AND FOUR DIMENSIONAL NMR SPECTROSCOPY
Method Solution NMR Resolution N.A. Mutation No [10]
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 .GDP or .GDP2 or .GDP3 or :3GDP;style chemicals stick;color identity;select .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:116 or .A:117 or .A:119 or .A:120 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)
GLY12
4.134
GLY13
2.262
VAL14
2.739
GLY15
1.983
LYS16
2.216
SER17
2.193
ALA18
2.493
LEU19
4.212
PHE28
2.678
VAL29
3.324
ASP30
2.248
GLU31
2.981
Residue
Distance (Å)
TYR32
4.187
ASP33
4.572
PRO34
4.326
ASN116
3.164
LYS117
2.004
ASP119
2.226
LEU120
1.703
SER145
2.997
ALA146
2.195
LYS147
2.000
THR148
4.897
PDB ID: 2CE2      CRYSTAL STRUCTURE ANALYSIS OF A FLUORESCENT FORM OF H-RAS P21 IN COMPLEX WITH GDP
Method X-ray diffraction Resolution 1.00 Å Mutation Yes [11]
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
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GDP or .GDP2 or .GDP3 or :3GDP;style chemicals stick;color identity;select .X:11 or .X:12 or .X:13 or .X:14 or .X:15 or .X:16 or .X:17 or .X:18 or .X:28 or .X:29 or .X:30 or .X:31 or .X:32 or .X:34 or .X:57 or .X:116 or .X:117 or .X:118 or .X:119 or .X:120 or .X:144 or .X:145 or .X:146 or .X:147; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ALA11
3.969
GLY12
4.025
GLY13
2.932
VAL14
3.431
GLY15
3.003
LYS16
2.720
SER17
3.003
ALA18
2.841
PHE28
3.042
VAL29
3.244
ASP30
2.910
GLU31
3.839
Residue
Distance (Å)
CYS32
3.557
PRO34
4.786
ASP57
4.655
ASN116
3.042
LYS117
2.939
SER118
4.939
ASP119
2.907
LEU120
3.386
THR144
4.546
SER145
3.506
ALA146
2.768
LYS147
3.687
PDB ID: 2CLD      CRYSTAL STRUCTURE ANALYSIS OF A FLUORESCENT FORM OF H-RAS P21 IN COMPLEX WITH GDP (2)
Method X-ray diffraction Resolution 1.22 Å Mutation Yes [11]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
33
PTIEDSYRKQ
43
VVIDGETCLL
53

DILDTAGQEE
63
YSAMRDQYMR
73
TGEGFLCVFA
83
INNTKSFEDI
93
HQYREQIKRV
103

KDSDDVPMVL
113
VGNKSDLAAR
123
TVESRQAQDL
133
ARSYGIPYIE
143
TSAKTRQGVE
153

DAFYTLVREI
163
RQH
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GDP or .GDP2 or .GDP3 or :3GDP;style chemicals stick;color identity;select .X:11 or .X:12 or .X:13 or .X:14 or .X:15 or .X:16 or .X:17 or .X:18 or .X:28 or .X:29 or .X:34 or .X:57 or .X:116 or .X:117 or .X:118 or .X:119 or .X:120 or .X:144 or .X:145 or .X:146 or .X:147; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ALA11
4.048
GLY12
4.007
GLY13
2.937
VAL14
3.216
GLY15
2.987
LYS16
2.890
SER17
3.082
ALA18
2.834
PHE28
3.378
VAL29
3.109
PRO34
4.354
Residue
Distance (Å)
ASP57
4.800
ASN116
3.214
LYS117
3.370
SER118
4.876
ASP119
2.928
LEU120
3.607
THR144
4.714
SER145
3.598
ALA146
2.923
LYS147
3.548
PDB ID: 2QUZ      Crystal Structure of the activating H-RasK117R mutant in Costello Syndrome, bound to Mg-GDP
Method X-ray diffraction Resolution 1.49 Å Mutation Yes [12]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHQYREQI
100

KRVKDSDDVP
110
MVLVGNRCDL
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 .GDP or .GDP2 or .GDP3 or :3GDP;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:34 or .A:57 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
3.797
GLY12
3.791
GLY13
2.771
VAL14
3.319
GLY15
2.991
LYS16
2.783
SER17
2.968
ALA18
2.758
PHE28
3.142
VAL29
3.818
ASP30
2.716
GLU31
4.544
Residue
Distance (Å)
TYR32
3.658
PRO34
4.912
ASP57
4.631
ASN116
3.101
ARG117
3.247
CYS118
4.652
ASP119
2.659
LEU120
3.415
THR144
4.561
SER145
3.384
ALA146
2.845
LYS147
3.458
PDB ID: 7JII      HRAS A59E GDP
Method X-ray diffraction Resolution 1.53 Å Mutation Yes [13]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTEG
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 .GDP or .GDP2 or .GDP3 or :3GDP;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:57 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
3.751
GLY12
3.739
GLY13
2.754
VAL14
3.358
GLY15
2.901
LYS16
2.627
SER17
2.931
ALA18
2.891
PHE28
3.249
VAL29
3.898
ASP30
3.501
GLU31
2.596
Residue
Distance (Å)
TYR32
4.028
ASP33
4.494
ASP57
4.665
ASN116
3.186
LYS117
3.250
CYS118
4.842
ASP119
2.754
LEU120
3.676
THR144
4.565
SER145
3.408
ALA146
2.931
LYS147
3.522
PDB ID: 1LF5      Crystal Structure of RasA59G in the GDP-bound Form
Method X-ray diffraction Resolution 1.70 Å Mutation Yes [14]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTGG
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 .GDP or .GDP2 or .GDP3 or :3GDP;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:57 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
3.814
GLY12
3.702
GLY13
2.711
VAL14
3.368
GLY15
3.026
LYS16
2.708
SER17
3.105
ALA18
2.789
PHE28
3.256
VAL29
2.886
ASP30
2.772
GLU31
4.349
Residue
Distance (Å)
TYR32
3.982
ASP57
4.819
ASN116
3.064
LYS117
3.158
CYS118
4.791
ASP119
2.812
LEU120
3.424
THR144
4.646
SER145
3.446
ALA146
2.869
LYS147
3.589
PDB ID: 1XJ0      Crystal Structure of the GDP-bound form of the RasG60A mutant
Method X-ray diffraction Resolution 1.70 Å Mutation Yes [15]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAA
60
QEEYSAMRDQ
70
YMRTGEGFLC
80
VFAINNTKSF
90
EDIHQYREQI
100

KRVKDSDDVP
110
MVLVGNKDLA
121
ARTVESRQAQ
131
DLARSYGIPY
141
IETSAKTRQG
151

VEDAFYTLVR
161
EIRQH
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GDP or .GDP2 or .GDP3 or :3GDP;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:34 or .A:57 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
3.819
GLY12
3.738
GLY13
2.742
VAL14
3.269
GLY15
2.968
LYS16
2.686
SER17
3.022
ALA18
2.795
PHE28
3.100
VAL29
3.464
ASP30
2.821
GLU31
4.721
Residue
Distance (Å)
TYR32
3.840
PRO34
4.930
ASP57
4.693
ASN116
3.114
LYS117
3.154
ASP119
2.762
LEU120
3.385
THR144
4.629
SER145
3.309
ALA146
2.707
LYS147
3.427
PDB ID: 2X1V      Crystal Structure of the activating H-Ras I163F mutant in Costello Syndrome, bound to MG-GDP
Method X-ray diffraction Resolution 1.70 Å Mutation Yes [16]
PDB Sequence
TEYKLVVVGA
11
GGVGKSALTI
21
QLIQNHFVDS
39
YRKQVVIDGE
49
TCLLDILDTA
59

EGFLCVFAIN
85
NTKSFEDIHQ
95
YREQIKRVKD
105
SDDVPMVLVG
115
NKCDLAARTV
125

ESRQAQDLAR
135
SYGIPYIETS
145
AKTRQGVEDA
155
FYTLVREFR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GDP or .GDP2 or .GDP3 or :3GDP;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:57 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
4.042
GLY12
4.276
GLY13
3.256
VAL14
3.556
GLY15
3.003
LYS16
2.682
SER17
2.643
ALA18
2.882
PHE28
3.212
VAL29
3.904
Residue
Distance (Å)
ASP57
4.545
ASN116
3.268
LYS117
3.238
CYS118
4.831
ASP119
2.810
LEU120
3.599
THR144
4.712
SER145
3.440
ALA146
2.898
LYS147
3.603
PDB ID: 6DZH      HRAS G13D bound to GDP (H13GDP)
Method X-ray diffraction Resolution 1.95 Å Mutation Yes [17]
PDB Sequence
MTEYKLVVVG
10
AGDVGKSALT
20
IQLIQNHFVD
30
EYDPTEDSYR
41
KQVVIDGETC
51

LLDILDTAGQ
61
EEYSAMRDQY
71
MRTGEGFLCV
81
FAINNTKSFE
91
DIHQYREQIK
101

RVKDSDDVPM
111
VLVGNKCDLA
121
ARTVESRQAQ
131
DLARSYGIPY
141
IETSAKTRQG
151

VEDAFYTLVR
161
EIRQH
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GDP or .GDP2 or .GDP3 or :3GDP;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:57 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
3.741
GLY12
3.865
ASP13
2.819
VAL14
3.331
GLY15
2.912
LYS16
2.553
SER17
3.042
ALA18
2.670
LEU19
4.987
PHE28
3.152
VAL29
2.974
ASP30
3.870
GLU31
3.585
Residue
Distance (Å)
TYR32
4.786
ASP33
4.411
ASP57
4.987
ASN116
3.152
LYS117
3.086
CYS118
4.870
ASP119
2.653
LEU120
3.594
THR144
4.745
SER145
3.495
ALA146
2.862
LYS147
3.375
PDB ID: 1ZVQ      Structure of the Q61G mutant of Ras in the GDP-bound form
Method X-ray diffraction Resolution 2.00 Å Mutation Yes [18]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
GEEYSAMRDQ
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 .GDP or .GDP2 or .GDP3 or :3GDP;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:34 or .A:57 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
3.785
GLY12
3.750
GLY13
2.755
VAL14
3.311
GLY15
3.030
LYS16
2.627
SER17
3.002
ALA18
2.735
PHE28
3.366
VAL29
2.887
ASP30
2.726
GLU31
4.309
Residue
Distance (Å)
TYR32
3.725
PRO34
4.852
ASP57
4.624
ASN116
3.160
LYS117
3.188
CYS118
4.802
ASP119
2.783
LEU120
3.444
THR144
4.689
SER145
3.457
ALA146
2.900
LYS147
3.530
PDB ID: 3KUD      Complex of Ras-GDP with RafRBD(A85K)
Method X-ray diffraction Resolution 2.15 Å Mutation Yes [19]
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
REIRQ
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GDP or .GDP2 or .GDP3 or :3GDP;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: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
3.881
GLY12
3.959
GLY13
2.869
VAL14
3.182
GLY15
3.105
LYS16
2.718
SER17
2.710
ALA18
2.713
LEU19
4.957
PHE28
3.519
VAL29
2.774
ASP30
3.279
GLU31
3.411
TYR32
3.319
Residue
Distance (Å)
ASP33
4.212
PRO34
4.901
THR35
4.102
ASP57
4.673
ASN116
3.221
LYS117
3.071
CYS118
4.884
ASP119
2.758
LEU120
3.546
THR144
4.565
SER145
3.453
ALA146
2.887
LYS147
3.633
PDB ID: 1WQ1      RAS-RASGAP COMPLEX
Method X-ray diffraction Resolution 2.50 Å Mutation No [20]
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 .GDP or .GDP2 or .GDP3 or :3GDP;style chemicals stick;color identity;select .R:11 or .R:12 or .R:13 or .R:14 or .R:15 or .R:16 or .R:17 or .R:18 or .R:19 or .R:28 or .R:29 or .R:30 or .R:31 or .R:33 or .R:35 or .R:57 or .R:116 or .R:117 or .R:119 or .R:120 or .R:144 or .R:145 or .R:146 or .R:147; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ALA11
4.072
GLY12
3.647
GLY13
2.662
VAL14
3.655
GLY15
3.009
LYS16
2.782
SER17
2.842
ALA18
2.793
LEU19
4.976
PHE28
3.152
VAL29
2.964
ASP30
3.303
Residue
Distance (Å)
GLU31
4.445
ASP33
4.452
THR35
3.652
ASP57
4.961
ASN116
3.011
LYS117
3.503
ASP119
3.066
LEU120
4.459
THR144
4.850
SER145
3.470
ALA146
2.890
LYS147
3.707
PDB ID: 3LO5      Crystal Structure of the dominant negative S17N mutant of Ras
Method X-ray diffraction Resolution 2.57 Å Mutation Yes [21]
PDB Sequence
MTEYKLVVVG
10
AGGVGKNALT
20
IQLIQNHFVD
38
SYRKQVVIDG
48
ETCLLDILDM
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
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GDP or .GDP2 or .GDP3 or :3GDP;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: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
4.035
GLY12
3.510
GLY13
2.536
VAL14
3.376
GLY15
2.956
LYS16
2.688
ASN17
3.125
ALA18
3.083
PHE28
2.973
VAL29
4.031
Residue
Distance (Å)
ASN116
3.098
LYS117
3.155
CYS118
4.737
ASP119
2.557
LEU120
3.387
THR144
4.548
SER145
3.216
ALA146
2.793
LYS147
3.516
PDB ID: 1XD2      Crystal Structure of a ternary Ras:SOS:Ras*GDP complex
Method X-ray diffraction Resolution 2.70 Å Mutation Yes [22]
PDB Sequence
MTEYKLVVVG
10
AGGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
QEEASAMRDQ
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 .GDP or .GDP2 or .GDP3 or :3GDP;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: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
3.855
GLY12
3.651
GLY13
2.662
VAL14
3.411
GLY15
2.986
LYS16
2.704
SER17
2.981
ALA18
2.777
PHE28
3.233
VAL29
2.525
ASP30
2.973
GLU31
3.860
TYR32
3.119
Residue
Distance (Å)
ASP33
4.246
THR35
3.865
ASP57
4.999
ASN116
3.098
LYS117
3.313
CYS118
4.862
ASP119
2.602
LEU120
3.434
THR144
4.435
SER145
3.258
ALA146
2.694
LYS147
3.487
PDB ID: 1PLL      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 [23]
PDB Sequence
MTEYKLVVVG
10
APGVGKSALT
20
IQLIQNHFVD
30
EYDPTIEDSY
40
RKQVVIDGET
50

CLLDILDTAG
60
YSAMRDQYMR
73
TGEGFLCVFA
83
INNTKSFEDI
93
HQYREQIKRV
103

KDSDDVPMVL
113
VGNKCDLAAR
123
TVESRQAQDL
133
ARSYGIYIET
144
SAKTRQGVED
154

AFYTLVREIR
164
QH
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GDP or .GDP2 or .GDP3 or :3GDP;style chemicals stick;color identity;select .A:11 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:33 or .A:34 or .A:35 or .A:57 or .A:58 or .A:59 or .A:60 or .A:117 or .A:119 or .A:120 or .A:144 or .A:145 or .A:146; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ALA11
3.759
GLY13
4.083
VAL14
2.973
GLY15
2.735
LYS16
3.212
SER17
3.492
ALA18
3.760
PHE28
3.411
VAL29
4.017
ASP30
3.862
ASP33
3.534
PRO34
3.068
Residue
Distance (Å)
THR35
4.706
ASP57
4.301
THR58
3.964
ALA59
3.832
GLY60
2.785
LYS117
3.182
ASP119
3.342
LEU120
4.487
THR144
3.137
SER145
2.644
ALA146
3.694
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 Regional polysterism in the GTP-bound form of the human c-Ha-Ras protein. Biochemistry. 1997 Jul 29;36(30):9109-19.
REF 3 Ras Binder Induces a Modified Switch-II Pocket in GTP and GDP States. Cell Chem Biol. 2017 Dec 21;24(12):1455-1466.e14.
REF 4 K-Ras(G12C) inhibitors allosterically control GTP affinity and effector interactions. Nature. 2013 Nov 28;503(7477):548-51.
REF 5 Selenomethionine incorporation into a protein by cell-free synthesis. J Struct Funct Genomics. 2002;2(1):29-35.
REF 6 Crystal structures at 2.2 A resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP. J Mol Biol. 1991 Feb 5;217(3):503-16.
REF 7 Inhibition of RAS function through targeting an allosteric regulatory site. Nat Chem Biol. 2017 Jan;13(1):62-68.
REF 8 HRAS G12S in complex with GDP
REF 9 Drugging all RAS isoforms with one pocket. Future Med Chem. 2020 Nov;12(21):1911-1923.
REF 10 Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy. Biochemistry. 1994 Mar 29;33(12):3515-31.
REF 11 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 12 Mutation analysis in Costello syndrome: functional and structural characterization of the HRAS p.Lys117Arg mutation. Hum Mutat. 2008 Feb;29(2):232-9.
REF 13 Regulation of GTPase function by autophosphorylation. Mol Cell. 2022 Mar 3;82(5):950-968.e14.
REF 14 The structural basis for the transition from Ras-GTP to Ras-GDP. Proc Natl Acad Sci U S A. 2002 Sep 17;99(19):12138-42.
REF 15 Structure of an intermediate for nucleotide exchange by Ras
REF 16 Crystal Structure of the Activating H-Ras I163F Mutant in Costello Syndrome, Bound to Mg-Gdp
REF 17 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.
REF 18 Structure of a transient intermediate for GTP hydrolysis by ras. Structure. 2006 Mar;14(3):427-36.
REF 19 What makes Ras an efficient molecular switch: a computational, biophysical, and structural study of Ras-GDP interactions with mutants of Raf. J Mol Biol. 2010 Jun 11;399(3):422-35.
REF 20 The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants. Science. 1997 Jul 18;277(5324):333-8.
REF 21 Structure of the dominant negative S17N mutant of Ras. Biochemistry. 2010 Mar 9;49(9):1970-4.
REF 22 Structural analysis of autoinhibition in the Ras activator Son of sevenless. Cell. 2004 Oct 29;119(3):393-405.
REF 23 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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