MolNFT v1 · #52506 · protein

RAC2 (G12V) in complex with GDP

2W2T · RAS-related C3 botulinum toxin substrate 2: “RAC2 (G12V) in complex with GDP”. X-ray diffraction, 2 ligands (GDP, MG), 1 pocket (best druggability 0.46). MolNFT v1 #52506 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2W2T
Type: protein
Length: 178 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RAS-related C3 botulinum toxin substrate 2
UniProt: P15153
Ligands: GDP, MG
Pockets: 1 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RAS-related C3 botulinum toxin substrate 2	protein	178	38% helix, 23% strand	P15153

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	121	0.46	0.78	30	MG, GDP

Compared structures

2W2T · Rac2 (G12V) in complex with GDP · the same entry in another collection · chain A against A, 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 0.97

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 2W2T · PDBe 2W2T · UniProt P15153

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