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 T96736 Target Info
Target Name Transforming protein RhoA (RHOA)
Synonyms h12; Rho cDNA clone 12; RHO12; ARHA; ARH12
Target Type Discontinued Target
Gene Name RHOA
Biochemical Class Small GTPase
UniProt ID
RHOA_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: 5C4M      RhoA GDP with novel switch II conformation
Method X-ray diffraction Resolution 1.30 Å Mutation Yes [1]
PDB Sequence
AIRKKLVIVG
12
DGACGKTCLL
22
IVNSKDQFPE
32
VYVPTVFENY
42
VADIEVDGKQ
52

VELALWDTAG
62
QEDYDRLRPL
72
SYPDTDVILM
82
CFSIDSPDSL
92
ENIPEKWTPE
102

VKHFCPNVPI
112
ILVGNKKDLR
122
NDEHTRRELA
132
KMKQEPVKPE
142
EGRDMANRIG
152

AFGYMECSAK
162
TKDGVREVFE
172
MATRAALQA
Residue
Distance (Å)
ASP13
3.890
GLY14
3.854
ALA15
2.780
CYS16
3.338
GLY17
3.036
LYS18
2.771
THR19
2.969
CYS20
2.790
LEU21
4.909
PHE30
3.530
PRO31
4.867
Residue
Distance (Å)
VAL35
3.540
PRO36
4.793
THR37
4.227
ASP59
4.949
LYS118
3.024
ASP120
2.793
LEU121
3.484
SER160
3.569
ALA161
2.983
LYS162
3.138
PDB ID: 6R3V      Crystal Structure of RhoA-GDP-Pi in Complex with RhoGAP
Method X-ray diffraction Resolution 1.75 Å Mutation No [2]
PDB Sequence
AAIRKKLVIV
11
GDGACGKTCL
21
LIVYVPTVFE
40
NYVADIEVDG
50
KQVELALWDT
60

AGQEDYDRLR
70
PLSYPDTDVI
80
LMCFSIDSPD
90
SLENIPEKWT
100
PEVKHFCPNV
110

PIILVGNKKD
120
LRNDEHTRRE
130
LAKMKQEPVK
140
PEEGRDMANR
150
IGAFGYMECS
160

AKTKDGVREV
170
FEMATRAALQ
180
AR
Residue
Distance (Å)
ASP13
3.799
GLY14
4.096
ALA15
2.898
CYS16
3.167
GLY17
3.039
LYS18
2.829
THR19
2.901
CYS20
2.749
LEU21
4.818
TYR34
3.451
Residue
Distance (Å)
VAL35
4.379
THR37
3.975
LYS118
3.133
LYS119
4.978
ASP120
2.771
LEU121
3.448
CYS159
4.955
SER160
3.478
ALA161
2.899
LYS162
3.233
PDB ID: 1OW3      Crystal Structure of RhoA.GDP.MgF3-in Complex with RhoGAP
Method X-ray diffraction Resolution 1.80 Å Mutation Yes [3]
PDB Sequence
AIRKKLVIVG
12
DGACGKTCLL
22
IVNSKDQFPE
32
VYVPTVFENY
42
VADIEVDGKQ
52

VELALWDTAG
62
QEDYDRLRPL
72
SYPDTDVILM
82
CFSIDSPDSL
92
ENIPEKWTPE
102

VKHFCPNVPI
112
ILVGNKKDLR
122
NDEHTRRELA
132
KMKQEPVKPE
142
EGRDMANRIG
152

AFGYMECSAK
162
TKDGVREVFE
172
MATRAALQA
Residue
Distance (Å)
ASP13
4.083
GLY14
4.122
ALA15
2.972
CYS16
3.285
GLY17
3.058
LYS18
2.729
THR19
2.958
CYS20
2.840
LEU21
4.959
PHE30
3.448
PRO31
4.903
Residue
Distance (Å)
VAL33
4.586
TYR34
3.581
VAL35
4.337
THR37
4.122
ASP59
4.863
LYS118
2.971
ASP120
2.764
LEU121
3.440
SER160
3.584
ALA161
2.963
LYS162
3.208
PDB ID: 1FTN      CRYSTAL STRUCTURE OF THE HUMAN RHOA/GDP COMPLEX
Method X-ray diffraction Resolution 2.10 Å Mutation Yes [4]
PDB Sequence
IRKKLVIVGD
13
GACGKTCLLI
23
VNSKDQFPEV
33
YVPTVFENYV
43
ADIEVDGKQV
53

ELALWDTAGQ
63
EDYDRLRPLS
73
YPDTDVILMC
83
FSIDSPDSLE
93
NIPEKWTPEV
103

KHFCPNVPII
113
LVGNKKDLRN
123
DEHTRRELAK
133
MKQEPVKPEE
143
GRDMANRIGA
153

FGYMECSAKT
163
KDGVREVFEM
173
ATRAALQ
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:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:21 or .A:30 or .A:35 or .A:36 or .A:37 or .A:59 or .A:63 or .A:118 or .A:120 or .A:121 or .A:160 or .A:161 or .A:162; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP13
3.870
GLY14
3.676
ALA15
2.631
CYS16
3.489
GLY17
2.961
LYS18
2.734
THR19
2.932
CYS20
2.870
LEU21
4.960
PHE30
3.437
VAL35
4.014
Residue
Distance (Å)
PRO36
4.833
THR37
4.249
ASP59
4.824
GLN63
4.499
LYS118
2.867
ASP120
2.707
LEU121
3.434
SER160
3.650
ALA161
3.095
LYS162
3.029
PDB ID: 5M70      Crystal Structure of human RhoGAP mutated in its arginin finger (R85A) in complex with RhoA.GDP.AlF4- human
Method X-ray diffraction Resolution 2.20 Å Mutation No [5]
PDB Sequence
RKKLVIVGDG
14
ACGKTCLLIV
24
NSKDQFPEVY
34
VPTVFENYVA
44
DIEVQVELAL
57

WDTAGQEDYD
67
RLRPLSYPDT
77
DVILMCFSID
87
SPDSLENIPE
97
KWTPEVKHFC
107

PNVPIILVGN
117
KKDLRNDEHT
127
RRELAKMKQE
137
PVKPEEGRDM
147
ANRIGAFGYM
157

ECSAKTKDGV
167
REVFEMATRA
177
AL
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 .B:13 or .B:14 or .B:15 or .B:16 or .B:17 or .B:18 or .B:19 or .B:20 or .B:21 or .B:30 or .B:31 or .B:34 or .B:35 or .B:37 or .B:59 or .B:63 or .B:118 or .B:120 or .B:121 or .B:159 or .B:160 or .B:161 or .B:162; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP13
4.213
GLY14
4.235
ALA15
3.064
CYS16
3.180
GLY17
2.774
LYS18
2.652
THR19
2.860
CYS20
2.981
LEU21
4.941
PHE30
3.499
PRO31
4.868
TYR34
3.379
Residue
Distance (Å)
VAL35
4.697
THR37
4.292
ASP59
4.864
GLN63
4.940
LYS118
3.261
ASP120
2.996
LEU121
3.600
CYS159
4.977
SER160
3.520
ALA161
2.853
LYS162
3.320
PDB ID: 5M6X      Crystal Structure of human RhoGAP mutated in its arginine finger (R85A) in complex with RhoA.GDP.MgF3- human
Method X-ray diffraction Resolution 2.40 Å Mutation Yes [5]
PDB Sequence
AIRKKLVIVG
12
DGACGKTCLL
22
IVNSKDQFPE
32
VYVPTVFENY
42
VADIEVDGKQ
52

VELALWDTAG
62
QEDYDRLRPL
72
SYPDTDVILM
82
CFSIDSPDSL
92
ENIPEKWTPE
102

VKHFCPNVPI
112
ILVGNKKDLR
122
NDEHTRRELA
132
KMKQEPVKPE
142
EGRDMANRIG
152

AFGYMECSAK
162
TKDGVREVFE
172
MATRAALQ
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 .B:13 or .B:14 or .B:15 or .B:16 or .B:17 or .B:18 or .B:19 or .B:20 or .B:30 or .B:31 or .B:34 or .B:35 or .B:37 or .B:59 or .B:118 or .B:120 or .B:121 or .B:160 or .B:161 or .B:162; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP13
3.927
GLY14
4.171
ALA15
3.002
CYS16
3.345
GLY17
3.074
LYS18
2.739
THR19
2.926
CYS20
2.894
PHE30
3.376
PRO31
4.743
Residue
Distance (Å)
TYR34
3.295
VAL35
4.473
THR37
4.313
ASP59
4.884
LYS118
2.792
ASP120
2.798
LEU121
3.609
SER160
3.534
ALA161
2.760
LYS162
3.289
PDB ID: 5FR2      Farnesylated RhoA-GDP in complex with RhoGDI-alpha, lysine acetylated at K178
Method X-ray diffraction Resolution 3.35 Å Mutation No [6]
PDB Sequence
MAAIRKKLVI
10
VGDGACGKTC
20
LLIVFSKDQF
30
PEVYVPTVFE
40
NYVADIEVDG
50

KQVELALWDT
60
AGQEDYDRLR
70
PLSYPDTDVI
80
LMCFSIDSPD
90
SLENIPEKWT
100

PEVKHFCPNV
110
PIILVGNKKD
120
LRNDEHTRRE
130
LAKMKQEPVK
140
PEEGRDMANR
150

IGAFGYMECS
160
AKTKDGVREV
170
FEMATRAALQ
180
AKKSGCL
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:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:21 or .A:30 or .A:35 or .A:36 or .A:37 or .A:59 or .A:117 or .A:118 or .A:119 or .A:120 or .A:121 or .A:159 or .A:160 or .A:161 or .A:162; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP13
3.816
GLY14
3.807
ALA15
2.765
CYS16
3.325
GLY17
3.053
LYS18
2.705
THR19
2.581
CYS20
3.022
LEU21
4.881
PHE30
3.642
VAL35
4.547
PRO36
4.041
Residue
Distance (Å)
THR37
4.114
ASP59
4.786
ASN117
4.912
LYS118
2.985
LYS119
4.953
ASP120
2.464
LEU121
3.338
CYS159
4.776
SER160
3.404
ALA161
2.771
LYS162
3.179
PDB ID: 5FR1      Double acetylated RhoGDI-alpha in complex with RhoA-GDP
Method X-ray diffraction Resolution 2.75 Å Mutation No [7]
PDB Sequence
IRKKLVIVGD
13
GACGKTCLLI
23
VFSKDQFPEV
33
YVPTVFENYV
43
ADIEVDGKQV
53

ELALWDTAGQ
63
EDYDRLRPLS
73
YPDTDVILMC
83
FSIDSPDSLE
93
NIPEKWTPEV
103

KHFCPNVPII
113
LVGNKKDLRN
123
DEHTRRELAK
133
MKQEPVKPEE
143
GRDMANRIGA
153

FGYMECSAKT
163
KDGVREVFEM
173
ATRAALQASG
189
CLVL
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:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:21 or .A:30 or .A:35 or .A:36 or .A:37 or .A:59 or .A:63 or .A:117 or .A:118 or .A:119 or .A:120 or .A:121 or .A:160 or .A:161 or .A:162 or .A:163; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP13
3.341
GLY14
3.377
ALA15
1.913
CYS16
2.507
GLY17
2.192
LYS18
1.892
THR19
1.922
CYS20
2.065
LEU21
4.363
PHE30
2.754
VAL35
2.820
PRO36
4.636
Residue
Distance (Å)
THR37
4.566
ASP59
4.865
GLN63
4.860
ASN117
4.673
LYS118
1.535
LYS119
4.990
ASP120
2.022
LEU121
2.182
SER160
2.948
ALA161
2.356
LYS162
2.392
THR163
4.845
PDB ID: 1CC0      CRYSTAL STRUCTURE OF THE RHOA.GDP-RHOGDI COMPLEX
Method X-ray diffraction Resolution 5.00 Å Mutation No [8]
PDB Sequence
IRKKLVIVGD
13
GACGKTCLLI
23
VNSKDQFPEV
33
YVPTVFENYV
43
ADIEVDGKQV
53

ELALWDTAGQ
63
EDYDRLRPLS
73
YPDTDVILMC
83
FSIDSPDSLE
93
NIPEKWTPEV
103

KHFCPNVPII
113
LVGNKKDLRN
123
DEHTRRELAK
133
MKQEPVKPEE
143
GRDMANRIGA
153

FGYMECSAKT
163
KDGVREVFEM
173
ATRAALQARR
183
GKKKSGC
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:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:21 or .A:30 or .A:35 or .A:36 or .A:37 or .A:59 or .A:63 or .A:118 or .A:120 or .A:121 or .A:160 or .A:161 or .A:162; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP13
3.870
GLY14
3.676
ALA15
2.630
CYS16
3.488
GLY17
2.961
LYS18
2.735
THR19
2.932
CYS20
2.869
LEU21
4.960
PHE30
3.437
VAL35
4.013
Residue
Distance (Å)
PRO36
4.833
THR37
4.249
ASP59
4.824
GLN63
4.498
LYS118
2.867
ASP120
2.707
LEU121
3.434
SER160
3.650
ALA161
3.095
LYS162
3.029
PDB ID: 5IRC      p190A GAP domain complex with RhoA
Method X-ray diffraction Resolution 1.72 Å Mutation Yes [9]
PDB Sequence
IRKKLVIVGD
13
GACGKTLLIV
24
NVYVPTVFEN
41
YVADIEVDGK
51
QVELALWDTA
61

GQEDYDRLRP
71
LSYPDTDVIL
81
MCFSIDSPDS
91
LENIPEKWTP
101
EVKHFCPNVP
111

IILVGNKKDL
121
RNDEHTRREL
131
AKMKQEPVKP
141
EEGRDMANRI
151
GAFGYMECSA
161

KTKDGVREVF
171
EMATRAALQ
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 .F:13 or .F:14 or .F:15 or .F:16 or .F:17 or .F:18 or .F:19 or .F:21 or .F:33 or .F:34 or .F:35 or .F:37 or .F:59 or .F:118 or .F:119 or .F:120 or .F:121 or .F:159 or .F:160 or .F:161 or .F:162; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP13
3.877
GLY14
4.010
ALA15
2.857
CYS16
3.295
GLY17
2.908
LYS18
2.750
THR19
3.034
LEU21
4.873
VAL33
4.704
TYR34
3.389
VAL35
4.396
Residue
Distance (Å)
THR37
4.131
ASP59
4.927
LYS118
2.931
LYS119
4.990
ASP120
2.732
LEU121
3.416
CYS159
4.968
SER160
3.541
ALA161
2.907
LYS162
3.212
PDB ID: 3LXR      Shigella IpgB2 in complex with human RhoA and GDP (complex C)
Method X-ray diffraction Resolution 1.68 Å Mutation No [10]
PDB Sequence
AAIRKKLVIV
11
GDGACGKTCL
21
LIVFSKDQFP
31
EVYVPTVFEN
41
YVADIEVDGK
51

QVELALWDTA
61
GQEDYDRLRP
71
LSYPDTDVIL
81
MCFSIDSPDS
91
LENIPEKWTP
101

EVKHFCPNVP
111
IILVGNKKDL
121
RNDEHTRREL
131
AKMKQEPVKP
141
EEGRDMANRI
151

GAFGYMECSA
161
KTKDGVREVF
171
EMATRAALQA
181
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:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:21 or .A:30 or .A:35 or .A:59 or .A:61 or .A:64 or .A:118 or .A:120 or .A:121 or .A:159 or .A:160 or .A:161 or .A:162; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP13
3.869
GLY14
3.874
ALA15
2.792
CYS16
3.364
GLY17
3.116
LYS18
2.880
THR19
2.816
CYS20
2.692
LEU21
4.857
PHE30
3.726
VAL35
3.727
Residue
Distance (Å)
ASP59
4.852
ALA61
3.971
GLU64
4.477
LYS118
3.111
ASP120
2.805
LEU121
3.480
CYS159
4.997
SER160
3.611
ALA161
2.951
LYS162
3.202
PDB ID: 3LW8      Shigella IpgB2 in complex with human RhoA, GDP and Mg2+ (complex A)
Method X-ray diffraction Resolution 1.85 Å Mutation No [10]
PDB Sequence
GPLGSAAIRK
6
KLVIVGDGAC
16
GKTCLLIVFS
26
KDQFPEVYVP
36
TVFENYVADI
46

EVDGKQVELA
56
LWDTAGQEDY
66
DRLRPLSYPD
76
TDVILMCFSI
86
DSPDSLENIP
96

EKWTPEVKHF
106
CPNVPIILVG
116
NKKDLRNDEH
126
TRRELAKMKQ
136
EPVKPEEGRD
146

MANRIGAFGY
156
MECSAKTKDG
166
VREVFEMATR
176
AALQA
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:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:21 or .A:30 or .A:35 or .A:63 or .A:118 or .A:120 or .A:121 or .A:160 or .A:161 or .A:162; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP13
3.733
GLY14
3.836
ALA15
2.747
CYS16
3.259
GLY17
3.095
LYS18
2.868
THR19
3.003
CYS20
2.777
LEU21
4.872
Residue
Distance (Å)
PHE30
3.532
VAL35
3.964
GLN63
4.656
LYS118
3.036
ASP120
2.730
LEU121
3.437
SER160
3.415
ALA161
3.078
LYS162
3.132
PDB ID: 4D0N      AKAP13 (AKAP-Lbc) RhoGEF domain in complex with RhoA
Method X-ray diffraction Resolution 2.10 Å Mutation No [11]
PDB Sequence
AIRKKLVIVG
12
DGACGKTCLL
22
IVFSKDQFPE
32
VYVPTVFENY
42
VADIEVDGKQ
52

VELALWDTAG
62
QEDYDRLRPL
72
SYPDTDVILM
82
CFSIDSPDSL
92
ENIPEKWTPE
102

VKHFCPNVPI
112
ILVGNKKDLR
122
NDEHTRRELA
132
KMKQEPVKPE
142
EGRDMANRIG
152

AFGYMECSAK
162
TKDGVREVFE
172
MATRAALQA
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:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:61 or .A:64 or .A:118 or .A:120 or .A:121 or .A:160 or .A:161 or .A:162; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP13
3.813
GLY14
3.748
ALA15
2.737
CYS16
3.354
GLY17
3.041
LYS18
2.912
THR19
3.009
CYS20
2.971
Residue
Distance (Å)
ALA61
3.695
GLU64
4.062
LYS118
2.754
ASP120
2.826
LEU121
3.539
SER160
3.567
ALA161
2.810
LYS162
3.293
PDB ID: 3LWN      Shigella IpgB2 in complex with human RhoA, GDP and Mg2+ (complex B)
Method X-ray diffraction Resolution 2.28 Å Mutation No [10]
PDB Sequence
SAAIRKKLVI
10
VGDGACGKTC
20
LLIVFSKDQF
30
PEVYVPTVFE
40
NYVADIEVDG
50

KQVELALWDT
60
AGQEDYDRLR
70
PLSYPDTDVI
80
LMCFSIDSPD
90
SLENIPEKWT
100

PEVKHFCPNV
110
PIILVGNKKD
120
LRNDEHTRRE
130
LAKMKQEPVK
140
PEEGRDMANR
150

IGAFGYMECS
160
AKTKDGVREV
170
FEMATRAALQ
180
A
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:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:21 or .A:30 or .A:35 or .A:59 or .A:61 or .A:64 or .A:118 or .A:120 or .A:121 or .A:159 or .A:160 or .A:161 or .A:162; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP13
3.623
GLY14
3.778
ALA15
2.743
CYS16
3.432
GLY17
3.081
LYS18
2.607
THR19
2.426
CYS20
2.610
LEU21
4.762
PHE30
3.868
VAL35
3.343
Residue
Distance (Å)
ASP59
4.709
ALA61
3.658
GLU64
4.482
LYS118
3.184
ASP120
2.565
LEU121
3.405
CYS159
4.958
SER160
3.499
ALA161
2.807
LYS162
3.164
PDB ID: 5HPY      Crystal Structure of RhoA.GDP.MgF3-in complex with human Myosin 9b RhoGAP domain
Method X-ray diffraction Resolution 2.40 Å Mutation Yes [12]
PDB Sequence
AIRKKLVIVG
12
DGACGKTCLL
22
IVNSKDQFPE
32
VYVPTVFENY
42
VADIEVDGKQ
52

VELALWDTAG
62
QEDYDRLRPL
72
SYPDTDVILM
82
CFSIDSPDSL
92
ENIPEKWTPE
102

VKHFCPNVPI
112
ILVGNKKDLR
122
NDEHTRRELA
132
KMKQEPVKPE
142
EGRDMANRIG
152

AFGYMECSAK
162
TKDGVREVFE
172
MATRAALQ
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 .B:13 or .B:14 or .B:15 or .B:16 or .B:17 or .B:18 or .B:19 or .B:20 or .B:21 or .B:30 or .B:31 or .B:34 or .B:35 or .B:37 or .B:59 or .B:118 or .B:119 or .B:120 or .B:121 or .B:160 or .B:161 or .B:162; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP13
3.915
GLY14
4.183
ALA15
3.039
CYS16
3.400
GLY17
3.019
LYS18
2.675
THR19
2.968
CYS20
2.833
LEU21
4.983
PHE30
3.575
PRO31
4.650
Residue
Distance (Å)
TYR34
3.612
VAL35
4.492
THR37
4.245
ASP59
4.813
LYS118
3.086
LYS119
4.990
ASP120
2.861
LEU121
3.368
SER160
3.406
ALA161
2.667
LYS162
3.185
PDB ID: 6V6U      Crystal structure of RhoA-GDP with novel Switch I conformation
Method X-ray diffraction Resolution 1.16 Å Mutation Yes [13]
PDB Sequence
AIRKKLVIVG
12
DGACGKTCLL
22
IVNSKDQFPE
32
VYVPTVFENY
42
VADIEVDGKQ
52

VELALWDTAG
62
QEDYDRLRPL
72
SYPDTDVILM
82
CFSIDSPDSL
92
ENIPEKWTPE
102

VKHFCPNVPI
112
ILVGNKKDLR
122
NDEHTRRELA
132
KMKQEPVKPE
142
EGRDMANRIG
152

AFGYMECSAK
162
TKDGVREVFE
172
MATRAALQA
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:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:21 or .A:34 or .A:35 or .A:36 or .A:59 or .A:63 or .A:118 or .A:119 or .A:120 or .A:121 or .A:159 or .A:160 or .A:161 or .A:162; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP13
3.789
GLY14
3.824
ALA15
2.762
CYS16
3.239
GLY17
3.036
LYS18
2.755
THR19
2.959
CYS20
2.767
LEU21
4.857
TYR34
3.872
VAL35
4.833
Residue
Distance (Å)
PRO36
4.104
ASP59
4.930
GLN63
4.866
LYS118
2.932
LYS119
4.945
ASP120
2.823
LEU121
3.485
CYS159
4.844
SER160
3.413
ALA161
2.889
LYS162
3.216
PDB ID: 6V6V      Crystal structure of oncogenic RhoA mutant G14V complexed with GDP
Method X-ray diffraction Resolution 1.40 Å Mutation Yes [13]
PDB Sequence
AIRKKLVIVG
12
DVACGKTCLL
22
IVNSKDQFPE
32
VYVPTVFENY
42
VADIEVDGKQ
52

VELALWDTAG
62
QEDYDRLRPL
72
SYPDTDVILM
82
CFSIDSPDSL
92
ENIPEKWTPE
102

VKHFCPNVPI
112
ILVGNKKDLR
122
NDEHTRRELA
132
KMKQEPVKPE
142
EGRDMANRIG
152

AFGYMECSAK
162
TKDGVREVFE
172
MATRAALQA
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:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:21 or .A:34 or .A:35 or .A:36 or .A:59 or .A:117 or .A:118 or .A:119 or .A:120 or .A:121 or .A:159 or .A:160 or .A:161 or .A:162; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP13
3.722
VAL14
3.770
ALA15
2.768
CYS16
3.294
GLY17
3.061
LYS18
2.766
THR19
2.971
CYS20
2.804
LEU21
4.930
TYR34
3.777
VAL35
4.834
Residue
Distance (Å)
PRO36
4.150
ASP59
4.933
ASN117
4.956
LYS118
2.872
LYS119
4.975
ASP120
2.810
LEU121
3.601
CYS159
4.836
SER160
3.415
ALA161
2.903
LYS162
3.229
PDB ID: 6KX2      Crystal structure of GDP bound RhoA protein
Method X-ray diffraction Resolution 1.45 Å Mutation Yes [14]
PDB Sequence
IRKKLVIVGD
13
GAVGKTSLLI
23
VFSKDQFPEV
33
YVPTVFENYV
43
ADIEVDGKQV
53

ELALWDTAGQ
63
EDYDRLRPLS
73
YPDTDVILMV
83
FSIDSPDSLE
93
NIPEKWTPEV
103

KHFCPNVPII
113
LVGNKKDLRN
123
DEHTRRELAK
133
MKQEPVKPEE
143
GRDMANRIGA
153

FGYMETSAKT
163
KDGVREVFEM
173
ATRAALQ
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:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:59 or .A:61 or .A:64 or .A:117 or .A:118 or .A:119 or .A:120 or .A:121 or .A:159 or .A:160 or .A:161 or .A:162; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP13
3.847
GLY14
4.038
ALA15
2.965
VAL16
3.375
GLY17
3.084
LYS18
2.769
THR19
2.763
SER20
2.721
ASP59
4.677
ALA61
3.360
Residue
Distance (Å)
GLU64
4.031
ASN117
3.171
LYS118
2.985
LYS119
4.805
ASP120
2.690
LEU121
3.489
THR159
4.486
SER160
3.255
ALA161
2.761
LYS162
3.437
PDB ID: 5EZ6      Crystallization and preliminary X-ray crystallographic analysis of a small GTPase RhoA
Method X-ray diffraction Resolution 1.80 Å Mutation No [15]
PDB Sequence
AAIRKKLVIV
11
GDGACGKTCL
21
LIVFSKDQFP
31
EVYVPTVFEN
41
YVADIEVDGK
51

QVELALWDTA
61
GQEDYDRLRP
71
LSYPDTDVIL
81
MCFSIDSPDS
91
LENIPEKWTP
101

EVKHFCPNVP
111
IILVGNKKDL
121
RNDEHTRREL
131
AKMKQEPVKP
141
EEGRDMANRI
151

GAFGYMECSA
161
KTKDGVREVF
171
EMATRAALQ
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 .B:13 or .B:14 or .B:15 or .B:16 or .B:17 or .B:18 or .B:19 or .B:20 or .B:21 or .B:59 or .B:61 or .B:64 or .B:118 or .B:120 or .B:121 or .B:159 or .B:160 or .B:161 or .B:162; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP13
3.755
GLY14
3.955
ALA15
2.847
CYS16
3.268
GLY17
3.085
LYS18
2.765
THR19
2.571
CYS20
2.734
LEU21
4.799
ASP59
4.647
Residue
Distance (Å)
ALA61
3.398
GLU64
4.089
LYS118
2.915
ASP120
2.841
LEU121
3.579
CYS159
4.944
SER160
3.472
ALA161
2.853
LYS162
3.239
PDB ID: 6KX3      Crystal structure of RhoA protein with covalent inhibitor DC-Rhoin
Method X-ray diffraction Resolution 1.98 Å Mutation Yes [14]
PDB Sequence
AIRKKLVIVG
12
DGAVGKTSLL
22
IVFSKDQFPE
32
VYVPTVFENY
42
VADIEVDGKQ
52

VELALWDTAG
62
QEDYPDTDVI
80
LMVFSIDSPD
90
SLENIPEKWT
100
PEVKHFCPNV
110

PIILVGNKKD
120
LRNDEHTRRE
130
LAKMKQEPVK
140
PEEGRDMANR
150
IGAFGYMETS
160

AKTKDGVREV
170
FEMATRAALQ
180
A
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:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:59 or .A:61 or .A:64 or .A:117 or .A:118 or .A:119 or .A:120 or .A:121 or .A:159 or .A:160 or .A:161 or .A:162; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP13
3.898
GLY14
3.905
ALA15
2.779
VAL16
3.390
GLY17
2.925
LYS18
2.728
THR19
3.027
SER20
2.659
ASP59
4.495
ALA61
3.708
Residue
Distance (Å)
GLU64
4.080
ASN117
3.192
LYS118
3.048
LYS119
4.722
ASP120
2.627
LEU121
3.545
THR159
4.457
SER160
3.213
ALA161
2.690
LYS162
3.448
PDB ID: 5A0F      Crystal structure of Yersinia Afp18-modified RhoA
Method X-ray diffraction Resolution 2.00 Å Mutation No [16]
PDB Sequence
AIRKKLVIVG
12
DGACGKTCLL
22
IVFSKDQFPE
32
VYVPTVFENY
42
VADIEVDGKQ
52

VELALWDTAG
62
QEDYDRLRPL
72
SYPDTDVILM
82
CFSIDSPDSL
92
ENIPEKWTPE
102

VKHFCPNVPI
112
ILVGNKKDLR
122
NDEHTRRELA
132
KMKQEPVKPE
142
EGRDMANRIG
152

AFGYMECSAK
162
TKDGVREVFE
172
MATRAALQ
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:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:21 or .A:59 or .A:61 or .A:64 or .A:118 or .A:120 or .A:121 or .A:159 or .A:160 or .A:161 or .A:162; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP13
3.841
GLY14
3.790
ALA15
2.747
CYS16
3.461
GLY17
3.033
LYS18
2.716
THR19
2.930
CYS20
2.727
LEU21
4.882
ASP59
4.947
Residue
Distance (Å)
ALA61
3.514
GLU64
4.000
LYS118
2.780
ASP120
2.849
LEU121
3.105
CYS159
4.853
SER160
3.555
ALA161
2.824
LYS162
3.273
PDB ID: 3MSX      Crystal structure of RhoA.GDP.MgF3 in complex with GAP domain of ArhGAP20
Method X-ray diffraction Resolution 1.65 Å Mutation Yes [17]
PDB Sequence
IRKKLVIVGD
13
GACGKTCLLI
23
VNSKDQFPEV
33
YVPTVFENYV
43
ADIEVDGKQV
53

ELALWDTAGQ
63
EDYDRLRPLS
73
YPDTDVILMC
83
FSIDSPDSLE
93
NIPEKWTPEV
103

KHFCPNVPII
113
LVGNKKDLRN
123
DEHTRRELAK
133
MKQEPVKPEE
143
GRDMANRIGA
153

FGYMECSAKT
163
KDGVREVFEM
173
ATRAALQ
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:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:21 or .A:30 or .A:31 or .A:33 or .A:34 or .A:35 or .A:37 or .A:59 or .A:118 or .A:119 or .A:120 or .A:121 or .A:159 or .A:160 or .A:161 or .A:162; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP13
3.968
GLY14
4.044
ALA15
2.902
CYS16
3.279
GLY17
2.988
LYS18
2.789
THR19
2.896
CYS20
2.844
LEU21
4.922
PHE30
3.412
PRO31
4.591
VAL33
5.000
Residue
Distance (Å)
TYR34
3.344
VAL35
4.152
THR37
4.160
ASP59
4.954
LYS118
3.001
LYS119
4.974
ASP120
2.776
LEU121
3.502
CYS159
4.993
SER160
3.429
ALA161
2.991
LYS162
3.248
PDB ID: 1DPF      CRYSTAL STRUCTURE OF A MG-FREE FORM OF RHOA COMPLEXED WITH GDP
Method X-ray diffraction Resolution 2.00 Å Mutation Yes [18]
PDB Sequence
AIRKKLVIVG
12
DVACGKTCLL
22
IVFSKDQFPA
32
VYVPTVFENY
42
VADIEVDGKQ
52

VELALWDTAG
62
QEDYDRARPL
72
SYPDTDVILM
82
CFSIDSPDSL
92
ENIPEKWTPE
102

VKHFCPNVPI
112
ILVGNKKDLR
122
NDEHTARELA
132
KMKQEPVKPA
142
EGRDMANRIG
152

AFGYMECSAK
162
TKDGVREVFE
172
MATRAALQ
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:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:21 or .A:59 or .A:61 or .A:64 or .A:117 or .A:118 or .A:120 or .A:121 or .A:159 or .A:160 or .A:161 or .A:162; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP13
4.377
VAL14
3.649
ALA15
2.565
CYS16
3.223
GLY17
2.599
LYS18
2.590
THR19
2.904
CYS20
2.892
LEU21
4.825
ASP59
4.612
Residue
Distance (Å)
ALA61
3.103
GLU64
3.921
ASN117
4.975
LYS118
3.030
ASP120
2.975
LEU121
3.215
CYS159
4.967
SER160
3.571
ALA161
2.780
LYS162
3.316
PDB ID: 5BWM      The complex structure of C3cer exoenzyme and GDP bound RhoA (NADH-bound state)
Method X-ray diffraction Resolution 2.50 Å Mutation Yes [19]
PDB Sequence
AIRKKLVIVG
12
DGACGKTCLL
22
IVNSKDQFPE
32
VYVPTVFENY
42
VADIEVDGKQ
52

VELALWDTAG
62
QEDYDRLRPL
72
SYPDTDVILM
82
CFSIDSPDSL
92
ENIPEKWTPE
102

VKHFCPNVPI
112
ILVGNKKDLR
122
NDEHTRRELA
132
KMKQEPVKPE
142
EGRDMANRIG
152

AFGYMECSAK
162
TKDGVREVFE
172
MATRAAL
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:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:21 or .A:30 or .A:35 or .A:36 or .A:37 or .A:59 or .A:118 or .A:119 or .A:120 or .A:121 or .A:159 or .A:160 or .A:161 or .A:162; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP13
3.609
GLY14
3.917
ALA15
2.842
CYS16
3.202
GLY17
3.117
LYS18
2.610
THR19
2.433
CYS20
2.793
LEU21
4.799
PHE30
3.703
VAL35
3.988
Residue
Distance (Å)
PRO36
4.813
THR37
4.060
ASP59
4.897
LYS118
2.268
LYS119
4.810
ASP120
2.625
LEU121
3.475
CYS159
4.933
SER160
3.333
ALA161
2.896
LYS162
3.144
PDB ID: 1TX4      RHO/RHOGAP/GDP(DOT)ALF4 COMPLEX
Method X-ray diffraction Resolution 1.65 Å Mutation Yes [20]
PDB Sequence
AIRKKLVIVG
12
DGACGKTCLL
22
IVNSKDQFYV
35
PTVFENYVAD
45
IEVDGKQVEL
55

ALWDTAGQED
65
YDRLRPLSYP
75
DTDVILMCFS
85
IDSPDSLENI
95
PEKWTPEVKH
105

FCPNVPIILV
115
GNKKDLRNDE
125
HTRRELAKMK
135
QEPVKPEEGR
145
DMANRIGAFG
155

YMECSAKTKD
165
GVREVFEMAT
175
RAAL
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 .B:13 or .B:14 or .B:15 or .B:16 or .B:17 or .B:18 or .B:19 or .B:20 or .B:21 or .B:30 or .B:34 or .B:35 or .B:37 or .B:59 or .B:63 or .B:118 or .B:120 or .B:121 or .B:159 or .B:160 or .B:161 or .B:162; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP13
4.075
GLY14
4.282
ALA15
3.061
CYS16
3.151
GLY17
2.976
LYS18
2.809
THR19
2.943
CYS20
2.845
LEU21
4.915
PHE30
3.380
TYR34
3.490
Residue
Distance (Å)
VAL35
4.490
THR37
4.508
ASP59
4.962
GLN63
4.855
LYS118
3.025
ASP120
2.777
LEU121
3.457
CYS159
4.954
SER160
3.596
ALA161
2.960
LYS162
3.201
References  Top
REF 1 RhoA GDP with novel switch II conformation
REF 2 A GAP-GTPase-GDP-P(i) Intermediate Crystal Structure Analyzed by DFT Shows GTP Hydrolysis Involves Serial Proton Transfers. Chemistry. 2019 Jun 26;25(36):8484-8488.
REF 3 MgF(3)(-) as a transition state analog of phosphoryl transfer. Chem Biol. 2002 Mar;9(3):375-81.
REF 4 Crystal structure of RhoA-GDP and its functional implications. Nat Struct Biol. 1997 Sep;4(9):699-703.
REF 5 Assessing the Influence of Mutation on GTPase Transition States by Using X-ray Crystallography, (19) F?NMR, and DFT Approaches. Angew Chem Int Ed Engl. 2017 Aug 7;56(33):9732-9735.
REF 6 Structural and Mechanistic Insights into the Regulation of the Fundamental Rho Regulator RhoGDI by Lysine Acetylation. J Biol Chem. 2016 Mar 11;291(11):5484-99.
REF 7 RhoGDIAlpha Acetylation at K127 and K141 Affects Binding toward Nonprenylated RhoA. Biochemistry. 2016 Jan 19;55(2):304-12.
REF 8 How RhoGDI binds Rho. Acta Crystallogr D Biol Crystallogr. 1999 Sep;55(Pt 9):1503-15.
REF 9 Deciphering the Molecular and Functional Basis of RHOGAP Family Proteins: A SYSTEMATIC APPROACH TOWARD SELECTIVE INACTIVATION OF RHO FAMILY PROTEINS. J Biol Chem. 2016 Sep 23;291(39):20353-71.
REF 10 Structure of Shigella IpgB2 in complex with human RhoA: implications for the mechanism of bacterial guanine nucleotide exchange factor mimicry. J Biol Chem. 2010 May 28;285(22):17197-208.
REF 11 The crystal structure of the RhoA-AKAP-Lbc DH-PH domain complex. Biochem J. 2014 Dec 1;464(2):231-9.
REF 12 Noncanonical Myo9b-RhoGAP Accelerates RhoA GTP Hydrolysis by a Dual-Arginine-Finger Mechanism. J Mol Biol. 2016 Jul 31;428(15):3043-57.
REF 13 Structure of an inactive conformation of GTP-bound RhoA GTPase. Structure. 2021 Jun 3;29(6):553-563.e5.
REF 14 Covalent Inhibitors Allosterically Block the Activation of Rho Family Proteins and Suppress Cancer Cell Invasion. Adv Sci (Weinh). 2020 May 13;7(14):2000098.
REF 15 Crystallization and preliminary X-ray crystallographic analysis of a small GTPase RhoA
REF 16 Tyrosine glycosylation of Rho by Yersinia toxin impairs blastomere cell behaviour in zebrafish embryos. Nat Commun. 2015 Jul 20;6:7807.
REF 17 Mechanism of molecular specificity of RhoGAP domains towards small GTPases of RhoA family.
REF 18 An open conformation of switch I revealed by the crystal structure of a Mg2+-free form of RHOA complexed with GDP. Implications for the GDP/GTP exchange mechanism. J Biol Chem. 2000 Jun 16;275(24):18311-7.
REF 19 Rho GTPase Recognition by C3 Exoenzyme Based on C3-RhoA Complex Structure. J Biol Chem. 2015 Aug 7;290(32):19423-32.
REF 20 Structure at 1.65 A of RhoA and its GTPase-activating protein in complex with a transition-state analogue. Nature. 1997 Oct 16;389(6652):758-62.

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