MolNFT v1 · #7647 · protein

Crystal structure of vav SH3 domain

1GCP · Vav proto-oncogene: “Crystal structure of vav SH3 domain”. X-ray diffraction, 1 pocket (best druggability 0.69). MolNFT v1 #7647 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1GCP
Type: protein
Length: 262 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Vav proto-oncogene
UniProt: P27870
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C, D	Vav proto-oncogene	protein	65	5% helix, 43% strand	P27870
B	Vav proto-oncogene	protein	67	4% helix, 45% strand	P27870

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	561	0.69	0.78	47	empty

Interfaces

4 interfaces between chains.

A–B · 427 Å² buried · 1 hydrogen bond · protein-protein
A–D · 408 Å² buried · 4 hydrogen bonds · protein-protein
B–D · 338 Å² buried · 11 hydrogen bonds · protein-protein
B–C · 328 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

1GCP · Crystal structure of vav SH3 domain · the same entry in another collection · chain A against A, TM-score 1.00
P27870 · AlphaFold monomer V2.0 prediction for proto-oncogene vav (P27870) · a predicted model of the same protein · chain B against A, TM-score 0.94

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 P27870
Elsewhere: RCSB PDB 1GCP · PDBe 1GCP · UniProt P27870

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