› 2nwm

Solution NMR

Solution structure of the first SH3 domain of human Vinexin and its interaction with the peptides from Vinculin

Released:
DOI: 10.2210/pdb2nwm/pdb
PDB entry 2nwm coloured by chain, ensemble of 20 models, front view.
PDB entry 2nwm coloured by chain, ensemble of 20 models, side view.
PDB entry 2nwm coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of the first SH3 domain of human vinexin and its interaction with vinculin peptides.
Zhang J, Li X, Yao B, Shen W, Sun H, Xu C, Wu J, Shi Y
Biochem Biophys Res Commun 357 931-7 (2007)
PMID: 17467669

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130008 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vinexin Chain: A
Molecule details ›
Chain: A
Length: 65 amino acids
Theoretical weight: 7.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O60504 (Residues: 383-438; Coverage: 8%)
Gene names: SCAM1, SORBS3
Sequence domains: Variant SH3 domain
Structure domains: SH3 Domains

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry, simulated annealing, molecular dynamics, torsion angle dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Survey of the year 2007 commercial optical biosensor literature.
Rich et al. (2008)
7 other articles

1 mention without citation

The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.
Chakraborty et al. (2013)