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 Phosphoaminophosphonic acid-guanylate ester Ligand Info
Canonical SMILES C1=NC2=C(N1C3C(C(C(O3)COP(=O)(O)OP(=O)(NP(=O)(O)O)O)O)O)N=C(NC2=O)N
InChI 1S/C10H17N6O13P3/c11-10-13-7-4(8(19)14-10)12-2-16(7)9-6(18)5(17)3(28-9)1-27-32(25,26)29-31(23,24)15-30(20,21)22/h2-3,5-6,9,17-18H,1H2,(H,25,26)(H3,11,13,14,19)(H4,15,20,21,22,23,24)/t3-,5-,6-,9-/m1/s1
InChIKey UQABYHGXWYXDTK-UUOKFMHZSA-N
PubChem Compound ID 135403657
Drug Binding Sites of Target  Top
PDB ID: 1KMQ      Crystal Structure of a Constitutively Activated RhoA Mutant (Q63L)
Method X-ray diffraction Resolution 1.55 Å Mutation Yes [1]
PDB Sequence
IRKKLVIVGD
13
GACGKTCLLI
23
VNSKDQFPEV
33
YVPTVFENYV
43
ADIEVDGKQV
53

ELALWDTAGL
63
EDYDRLRPLS
73
YPDTDVILMC
83
FSIDSPDSLE
93
NIPEKWTPEV
103

KHFCPNVPII
113
LVGNKKDLRN
123
DEHTRRELAK
133
MKQEPVKPEE
143
GRDMANRIGA
153

FGYMECSAKT
163
KDGVREVFEM
173
ATRAALQ
Residue
Distance (Å)
GLY12
4.670
ASP13
3.824
GLY14
3.569
ALA15
3.050
CYS16
3.192
GLY17
3.091
LYS18
2.669
THR19
2.960
CYS20
2.855
LEU21
4.882
PHE30
3.729
PRO31
4.705
TYR34
2.631
VAL35
4.564
Residue
Distance (Å)
PRO36
3.494
THR37
2.889
ASP59
4.924
THR60
4.236
ALA61
3.947
GLY62
2.819
LEU63
4.315
LYS118
2.967
ASP120
2.829
LEU121
3.595
CYS159
4.993
SER160
3.569
ALA161
2.971
LYS162
3.217
PDB ID: 6V6M      Crystal structure of an inactive state of GMPPNP-bound RhoA
Method X-ray diffraction Resolution 1.39 Å Mutation Yes [2]
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)
GLY12
4.708
ASP13
3.984
GLY14
3.576
ALA15
2.963
CYS16
3.390
GLY17
3.036
LYS18
2.840
THR19
2.877
CYS20
2.822
LEU21
4.991
TYR34
3.833
VAL35
4.901
PRO36
2.789
THR37
4.774
Residue
Distance (Å)
ASP59
4.922
THR60
4.143
ALA61
3.892
GLY62
2.846
GLN63
4.215
ASN117
4.992
LYS118
2.907
LYS119
4.981
ASP120
2.885
LEU121
3.545
CYS159
4.905
SER160
3.412
ALA161
2.850
LYS162
3.184
PDB ID: 1S1C      Crystal structure of the complex between the human RhoA and Rho-binding domain of human ROCKI
Method X-ray diffraction Resolution 2.60 Å Mutation No [3]
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
4.630
ASP13
3.783
GLY14
3.245
ALA15
2.968
CYS16
3.178
GLY17
3.093
LYS18
2.727
THR19
2.915
CYS20
2.818
LEU21
4.794
PHE30
3.460
PRO31
4.255
GLU32
4.670
TYR34
2.835
Residue
Distance (Å)
VAL35
4.723
PRO36
3.532
THR37
3.053
ASP59
4.896
THR60
4.154
ALA61
4.003
GLY62
2.885
GLN63
3.761
LYS118
3.091
ASP120
2.937
LEU121
3.436
SER160
3.473
ALA161
2.884
LYS162
3.200
References  Top
REF 1 Structure of a constitutively activated RhoA mutant (Q63L) at 1.55 A resolution. Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):876-80.
REF 2 Structure of an inactive conformation of GTP-bound RhoA GTPase. Structure. 2021 Jun 3;29(6):553-563.e5.
REF 3 Structural insights into the interaction of ROCKI with the switch regions of RhoA. J Biol Chem. 2004 Feb 20;279(8):7098-104.

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