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 5'-Guanosine-Diphosphate-Monothiophosphate Ligand Info
Canonical SMILES C1=NC2=C(N1C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OP(=S)(O)O)O)O)N=C(NC2=O)N
InChI 1S/C10H16N5O13P3S/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(26-9)1-25-29(19,20)27-30(21,22)28-31(23,24)32/h2-3,5-6,9,16-17H,1H2,(H,19,20)(H,21,22)(H2,23,24,32)(H3,11,13,14,18)/t3-,5-,6-,9-/m1/s1
InChIKey XOFLBQFBSOEHOG-UUOKFMHZSA-N
PubChem Compound ID 135398675
Drug Binding Sites of Target  Top
PDB ID: 6BCB      A Complex between PH Domain of p114RhoGEF and Activated RhoA Bound to a GTP Analog
Method X-ray diffraction Resolution 1.40 Å Mutation No [1]
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
A
Residue
Distance (Å)
GLY12
3.974
ASP13
3.414
GLY14
2.543
ALA15
2.206
CYS16
2.833
GLY17
2.348
LYS18
1.007
THR19
2.106
CYS20
1.972
LEU21
4.262
PHE30
2.445
PRO31
4.610
GLU32
4.742
TYR34
2.228
VAL35
3.973
PRO36
2.903
Residue
Distance (Å)
THR37
2.018
ASP59
4.868
THR60
4.084
ALA61
3.723
GLY62
2.070
GLN63
3.538
ASN117
4.764
LYS118
2.689
LYS119
4.883
ASP120
1.908
LEU121
2.570
SER160
3.043
ALA161
2.653
LYS162
2.320
THR163
4.696
PDB ID: 6BCA      A Complex between PH Domain of LbcRhoGEF (AKAP-Lbc) and Activated RhoA Bound to a GTP Analog
Method X-ray diffraction Resolution 2.00 Å Mutation No [1]
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
Residue
Distance (Å)
GLY12
4.037
ASP13
3.512
GLY14
2.783
ALA15
2.198
CYS16
2.894
GLY17
2.383
LYS18
1.291
THR19
2.045
CYS20
2.007
LEU21
4.229
PHE30
2.264
PRO31
4.579
TYR34
2.306
VAL35
3.857
PRO36
2.713
Residue
Distance (Å)
THR37
1.890
ASP59
4.831
THR60
4.168
ALA61
3.780
GLY62
2.103
GLN63
3.454
ASN117
4.803
LYS118
2.327
LYS119
4.815
ASP120
1.791
LEU121
2.685
SER160
3.005
ALA161
2.583
LYS162
2.310
THR163
4.634
PDB ID: 6BC0      A Complex between PH Domain of p190RhoGEF and Activated RhoA Bound to a GTP Analog
Method X-ray diffraction Resolution 2.20 Å Mutation No [2]
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
Residue
Distance (Å)
GLY12
4.028
ASP13
3.474
GLY14
2.371
ALA15
2.247
CYS16
3.058
GLY17
2.318
LYS18
1.207
THR19
2.248
CYS20
1.932
LEU21
4.297
PHE30
2.493
PRO31
4.022
GLU32
4.872
TYR34
2.520
VAL35
4.090
PRO36
3.140
Residue
Distance (Å)
THR37
2.150
ASP59
4.855
THR60
3.928
ALA61
3.538
GLY62
1.916
GLN63
3.261
ASN117
4.166
LYS118
2.171
LYS119
4.793
ASP120
1.992
LEU121
2.046
CYS159
4.824
SER160
2.935
ALA161
2.426
LYS162
2.932
PDB ID: 1CXZ      CRYSTAL STRUCTURE OF HUMAN RHOA COMPLEXED WITH THE EFFECTOR DOMAIN OF THE PROTEIN KINASE PKN/PRK1
Method X-ray diffraction Resolution 2.20 Å Mutation Yes [3]
PDB Sequence
SMAAIRKKLV
9
IVGDVACGKT
19
CLLIVFSKDQ
29
FPEVYVPTVF
39
ENYVADIEVD
49

GKQVELALWD
59
TAGQEDYDRL
69
RPLSYPDTDV
79
ILMCFSIDSP
89
DSLENIPEKW
99

TPEVKHFCPN
109
VPIILVGNKK
119
DLRNDEHTRR
129
ELAKMKQEPV
139
KPEEGRDMAN
149

RIGAFGYMEC
159
SAKTKDGVRE
169
VFEMATRAAL
179
QA
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GSP or .GSP2 or .GSP3 or :3GSP;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:20 or .A:21 or .A:30 or .A:31 or .A:34 or .A:35 or .A:36 or .A:37 or .A:59 or .A:60 or .A:61 or .A:62 or .A:63 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)
GLY12
4.671
ASP13
3.766
VAL14
3.532
ALA15
3.085
CYS16
3.227
GLY17
3.140
LYS18
2.630
THR19
2.788
CYS20
2.893
LEU21
4.832
PHE30
3.392
PRO31
4.898
TYR34
2.926
VAL35
4.365
Residue
Distance (Å)
PRO36
3.662
THR37
2.737
ASP59
4.847
THR60
4.308
ALA61
4.069
GLY62
2.990
GLN63
4.233
LYS118
2.969
ASP120
2.810
LEU121
3.711
CYS159
4.947
SER160
3.544
ALA161
2.887
LYS162
3.227
PDB ID: 1A2B      HUMAN RHOA COMPLEXED WITH GTP ANALOGUE
Method X-ray diffraction Resolution 2.40 Å Mutation Yes [4]
PDB Sequence
IRKKLVIVGD
13
VACGKTCLLI
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
ATRAALQA
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GSP or .GSP2 or .GSP3 or :3GSP;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:20 or .A:30 or .A:31 or .A:34 or .A:35 or .A:36 or .A:37 or .A:60 or .A:61 or .A:62 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 #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY12
4.791
ASP13
3.621
VAL14
3.764
ALA15
2.828
CYS16
2.761
GLY17
3.003
LYS18
2.903
THR19
3.005
CYS20
3.071
PHE30
3.958
PRO31
4.620
TYR34
2.916
VAL35
4.508
PRO36
3.741
Residue
Distance (Å)
THR37
3.097
THR60
4.359
ALA61
4.102
GLY62
3.113
GLN63
4.728
LYS118
3.234
LYS119
4.963
ASP120
3.007
LEU121
3.274
CYS159
4.914
SER160
3.576
ALA161
2.939
LYS162
3.422
PDB ID: 3KZ1      Crystal Structure of the Complex of PDZ-RhoGEF DH/PH domains with GTP-gamma-S Activated RhoA
Method X-ray diffraction Resolution 2.70 Å Mutation No [5]
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 .GSP or .GSP2 or .GSP3 or :3GSP;style chemicals stick;color identity;select .E:12 or .E:13 or .E:14 or .E:15 or .E:16 or .E:17 or .E:18 or .E:19 or .E:20 or .E:21 or .E:30 or .E:32 or .E:34 or .E:35 or .E:36 or .E:37 or .E:59 or .E:60 or .E:61 or .E:62 or .E:63 or .E:118 or .E:119 or .E:120 or .E:121 or .E:160 or .E:161 or .E:162; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY12
4.820
ASP13
3.667
GLY14
3.759
ALA15
2.888
CYS16
3.303
GLY17
2.968
LYS18
2.792
THR19
2.760
CYS20
2.893
LEU21
4.858
PHE30
3.552
GLU32
4.949
TYR34
3.254
VAL35
4.302
Residue
Distance (Å)
PRO36
3.908
THR37
2.834
ASP59
4.929
THR60
4.002
ALA61
3.940
GLY62
2.967
GLN63
4.229
LYS118
3.044
LYS119
4.949
ASP120
2.890
LEU121
3.443
SER160
3.811
ALA161
2.987
LYS162
3.028
PDB ID: 4XSG      The complex structure of C3cer exoenzyme and GTP bound RhoA (NADH-free state)
Method X-ray diffraction Resolution 1.80 Å Mutation Yes [6]
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
ATRAAL
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GSP or .GSP2 or .GSP3 or :3GSP;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:20 or .A:21 or .A:30 or .A:31 or .A:35 or .A:36 or .A:37 or .A:59 or .A:60 or .A:61 or .A:62 or .A:63 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)
GLY12
4.732
ASP13
3.826
GLY14
3.671
ALA15
2.861
CYS16
3.361
GLY17
3.109
LYS18
2.729
THR19
2.820
CYS20
2.883
LEU21
4.923
PHE30
3.404
PRO31
4.529
VAL35
3.808
PRO36
4.637
Residue
Distance (Å)
THR37
2.903
ASP59
4.947
THR60
3.948
ALA61
3.866
GLY62
2.867
GLN63
4.108
LYS118
2.985
ASP120
2.801
LEU121
3.512
CYS159
4.969
SER160
3.600
ALA161
2.929
LYS162
3.144
PDB ID: 4XSH      The complex structure of C3cer exoenzyme and GTP bound RhoA (NADH-bound state)
Method X-ray diffraction Resolution 2.50 Å Mutation Yes [6]
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 .GSP or .GSP2 or .GSP3 or :3GSP;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:20 or .A:21 or .A:30 or .A:31 or .A:35 or .A:36 or .A:37 or .A:38 or .A:59 or .A:60 or .A:61 or .A:62 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)
GLY12
4.867
ASP13
4.041
GLY14
3.612
ALA15
2.913
CYS16
3.736
GLY17
3.012
LYS18
2.585
THR19
2.789
CYS20
2.997
LEU21
4.903
PHE30
3.451
PRO31
4.716
VAL35
4.121
PRO36
4.696
Residue
Distance (Å)
THR37
2.934
VAL38
4.997
ASP59
4.938
THR60
3.963
ALA61
3.908
GLY62
2.944
GLN63
3.626
LYS118
3.048
ASP120
2.893
LEU121
3.484
SER160
3.649
ALA161
3.008
LYS162
3.103
References  Top
REF 1 Crystal structures of the PH domains from Lbc family of RhoGEFs bound to activated RhoA GTPase. Data Brief. 2018 Feb 20;17:356-362.
REF 2 Direct regulation of p190RhoGEF by activated Rho and Rac GTPases. J Struct Biol. 2018 Apr;202(1):13-24.
REF 3 The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1. Mol Cell. 1999 Nov;4(5):793-803.
REF 4 Crystal structure of human RhoA in a dominantly active form complexed with a GTP analogue. J Biol Chem. 1998 Apr 17;273(16):9656-66.
REF 5 Activated RhoA binds to the pleckstrin homology (PH) domain of PDZ-RhoGEF, a potential site for autoregulation. J Biol Chem. 2010 Jul 2;285(27):21070-81.
REF 6 Rho GTPase Recognition by C3 Exoenzyme Based on C3-RhoA Complex Structure. J Biol Chem. 2015 Aug 7;290(32):19423-32.

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