› 1gcp

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURE OF VAV SH3 DOMAIN

Released:
DOI: 10.2210/pdb1gcp/pdb
PDB entry 1gcp coloured by chain, front view.
PDB entry 1gcp coloured by chain, side view.
PDB entry 1gcp coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Novel recognition mode between Vav and Grb2 SH3 domains.
Nishida M, Nagata K, Hachimori Y, Horiuchi M, Ogura K, Mandiyan V, Schlessinger J, Inagaki F
EMBO J 20 2995-3007 (2001)
PMID: 11406576

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151089 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Proto-oncogene vav Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 70 amino acids
Theoretical weight: 8.03 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P27870 (Residues: 595-660; Coverage: 8%)
Gene names: Vav, Vav1
Sequence domains: SH3 domain
Structure domains: SH3 Domains

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU ULTRAX 18
Spacegroup: P21
Unit cell:
a: 32.205Å b: 101.115Å c: 39.707Å
α: 90° β: 91.34° γ: 90°
R-values:
R R work R free
0.198 0.193 0.253
Expression system: Escherichia coli

Quick links

Citations

15 review citations

Specificity and versatility of SH3 and other proline-recognition domains: structural basis and implications for cellular signal transduction.
Li SS. (2005)
14 more

9 mentions without citation

Protein-protein docking benchmark version 3.0.
Hwang et al. (2008)
8 more