Research workbench

RAC2 (G12V) in complex with gtpgs

Analyse RAC2 (G12V) in complex with gtpgs in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2W2V
Type: protein
Length: 676 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RAS-related C3 botulinum toxin substrate 2
UniProt: P15153
Ligands: GTP
Pockets: 7 · best druggability 0.56

Structure

x-ray diffraction · 4 distinct chains · 38% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RAS-related C3 botulinum toxin substrate 2	protein	171	39% helix, 22% strand	P15153
B	RAS-related C3 botulinum toxin substrate 2	protein	170	38% helix, 24% strand	P15153
C	RAS-related C3 botulinum toxin substrate 2	protein	161	36% helix, 22% strand	P15153
D	RAS-related C3 botulinum toxin substrate 2	protein	174	39% helix, 22% strand	P15153

Ligands and binding sites

GTP · Guanosine-5'-triphosphate · ligand · 4 copies · chains A, B, C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	317	0.56	0.75	37	empty
2	134	0.48	0.78	30	GTP
3	121	0.47	0.79	30	GTP
4	124	0.46	0.78	31	GTP
5	123	0.46	0.78	27	GTP

Interfaces

2 interfaces between chains.

A–B · 470 Å² buried · 9 hydrogen bonds · protein-protein
B–C · 142 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

2W2V · Rac2 (G12V) in complex with GTPgS · the same entry in another collection · chain D against D, TM-score 1.00
P15153 · AlphaFold monomer V2.0 prediction for RAS-related C3 botulinum toxin substrate 2 (P15153) · a predicted model of the same protein · chain A against A, TM-score 0.98

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P15153
Elsewhere: RCSB PDB 2W2V · PDBe 2W2V · UniProt P15153

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