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Apo structure of the activated truncation of VAV1

Analyse Apo structure of the activated truncation of VAV1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6NEW
Type: protein
Length: 389 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Proto-oncogene vav
UniProt: P15498
Ligands: ZN
Pockets: 3 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Proto-oncogene vav	protein	389	55% helix, 17% strand	P15498

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A

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

Pockets

3 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	114	0.59	0.85	22	empty
2	104	0.46	0.79	19	empty
3	113	0.39	0.75	19	empty

Compared structures

6NEW · Apo structure of the activated truncation of Vav1 · the same entry in another collection · chain A against A, TM-score 1.00
P15498 · AlphaFold monomer V2.0 prediction for proto-oncogene vav (P15498) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P15498
Elsewhere: RCSB PDB 6NEW · PDBe 6NEW · UniProt P15498

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