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 T88752 Target Info
Target Name Ras-related C3 botulinum toxin substrate 1 (RAC1)
Synonyms Cell migration-inducing gene5 protein
Target Type Literature-reported Target
Gene Name RAC1
Biochemical Class Small GTPase
UniProt ID
RAC1_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: 6BC1      A Complex between PH Domain of p190RhoGEF and Activated Rac1 Bound to a GTP Analog
Method X-ray diffraction Resolution 2.90 Å Mutation No [1]
PDB Sequence
PQAIKCVVVG
10
DGAVGKTCLL
20
ISYTTNAFPG
30
EYIPTVFDNY
40
SANVMVDGKP
50

VNLGLWDTAG
60
QEDYDRLRPL
70
SYPQTDVFLI
80
CFSLVSPASF
90
ENVRAKWYPE
100

VRHHCPNTPI
110
ILVGTKLDLR
120
DDKDTIEKLK
130
EKKLTPITYP
140
QGLAMAKEIG
150

AVKYLECSAL
160
TQRGLKTVFD
170
EAIRAVL
Residue
Distance (Å)
GLY10
4.431
ASP11
3.573
GLY12
2.751
ALA13
2.002
VAL14
3.100
GLY15
2.195
LYS16
1.655
THR17
2.202
CYS18
1.746
LEU19
4.220
PHE28
2.823
PRO29
4.576
TYR32
1.981
ILE33
4.173
PRO34
2.804
Residue
Distance (Å)
THR35
2.059
ASP57
4.659
THR58
3.716
ALA59
3.458
GLY60
2.243
GLN61
3.673
THR115
4.881
LYS116
2.526
LEU117
4.522
ASP118
2.489
LEU119
2.274
SER158
2.805
ALA159
2.092
LEU160
2.650
THR161
4.947
PDB ID: 4GZM      Crystal structure of RAC1 F28L mutant
Method X-ray diffraction Resolution 2.80 Å Mutation Yes [2]
PDB Sequence
IKCVVVGDGA
13
VGKTCLLISY
23
TTNALPGEYI
33
PTVFDNYSAN
43
VMVDGKPVNL
53

GLWDTAGQED
63
YDRLRPLSYP
73
QTDVFLICFS
83
LVSPASFENV
93
RAKWYPEVRH
103

HCPNTPIILV
113
GTKLDLRDDK
123
DTIEKLKEKK
133
LTPITYPQGL
143
AMAKEIGAVK
153

YLECSALTQR
163
GLKTVFDEAI
173
RAVL
Residue
Distance (Å)
GLY10
4.829
ASP11
3.610
GLY12
3.191
ALA13
3.096
VAL14
3.111
GLY15
2.903
LYS16
2.719
THR17
2.589
CYS18
2.775
LEU19
4.875
LEU28
4.845
PRO29
4.702
TYR32
2.913
ILE33
4.547
Residue
Distance (Å)
PRO34
3.641
THR35
3.230
ASP57
4.471
THR58
3.646
ALA59
4.583
GLY60
3.685
LYS116
3.802
ASP118
3.058
LEU119
3.425
CYS157
4.733
SER158
3.351
ALA159
2.662
LEU160
3.392
PDB ID: 2FJU      Activated Rac1 bound to its effector phospholipase C beta 2
Method X-ray diffraction Resolution 2.20 Å Mutation No [3]
PDB Sequence
MQAIKCVVVG
10
DGAVGKTCLL
20
ISYTTNAFPG
30
EYIPTVFDNY
40
SANVMVDGKP
50

VNLGLWDTAG
60
QEDYDRLRPL
70
SYPQTDVFLI
80
CFSLVSPASF
90
ENVRAKWYPE
100

VRHHCPNTPI
110
ILVGTKLDLR
120
DDKDTIEKLK
130
EKKLTPITYP
140
QGLAMAKEIG
150

AVKYLECSAL
160
TQRGLKTVFD
170
EAIRAVL
Residue
Distance (Å)
GLY10
4.720
ASP11
3.784
GLY12
3.417
ALA13
2.955
VAL14
3.452
GLY15
3.075
LYS16
2.742
THR17
2.804
CYS18
2.796
LEU19
4.745
PHE28
3.280
PRO29
4.923
TYR32
3.008
ILE33
4.548
Residue
Distance (Å)
PRO34
3.832
THR35
2.888
ASP57
4.771
THR58
4.134
ALA59
3.954
GLY60
2.822
GLN61
4.202
LYS116
3.275
ASP118
2.808
LEU119
3.311
CYS157
4.971
SER158
3.573
ALA159
2.855
LEU160
3.347
References  Top
REF 1 Direct regulation of p190RhoGEF by activated Rho and Rac GTPases. J Struct Biol. 2018 Apr;202(1):13-24.
REF 2 RAC1P29S is a spontaneously activating cancer-associated GTPase. Proc Natl Acad Sci U S A. 2013 Jan 15;110(3):912-7.
REF 3 Crystal structure of Rac1 bound to its effector phospholipase C-beta2. Nat Struct Mol Biol. 2006 Dec;13(12):1135-40.

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