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Solution structure of the ch domain from human vav-3 protein

Analyse Solution structure of the ch domain from human vav-3 protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2D86
Type: protein
Length: 143 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Vav-3 protein
UniProt: Q9UKW4
Pockets: 1 · best druggability 0.35

Structure

solution nmr · 1 distinct chain · 51% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Vav-3 protein	protein	143	51% helix, 0% strand	Q9UKW4

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	77	0.35	0.76	14	empty

Compared structures

2D86 · Solution structure of the CH domain from human Vav-3 protein · the same entry in another collection · chain A against A, TM-score 1.00
Q9UKW4 · AlphaFold monomer V2.0 prediction for guanine nucleotide exchange factor VAV3 (Q9UKW4) · a predicted model of the same protein · chain A against A, TM-score 0.87

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 Q9UKW4
Elsewhere: RCSB PDB 2D86 · PDBe 2D86 · UniProt Q9UKW4

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