› 2vil

Solution NMR

REFINED STRUCTURE OF THE ACTIN-SEVERING DOMAIN VILLIN 14T, DETERMINED BY SOLUTION NMR, 11 STRUCTURES

Released:
DOI: 10.2210/pdb2vil/pdb
PDB entry 2vil coloured by chain, ensemble of 11 models, front view.
PDB entry 2vil coloured by chain, ensemble of 11 models, side view.
PDB entry 2vil coloured by chain, ensemble of 11 models, top view.
Source organism: Gallus gallus
Primary publication:
Refined structure of villin 14T and a detailed comparison with other actin-severing domains.
Markus MA, Matsudaira P, Wagner G
Protein Sci 6 1197-209 (1997)
PMID: 9194180

Function and Biology Details

Biochemical function:
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-135979 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Villin-1 Chain: A
Molecule details ›
Chain: A
Length: 126 amino acids
Theoretical weight: 14.17 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P02640 (Residues: 2-127; Coverage: 15%)
Gene names: VIL, VIL1
Sequence domains: Gelsolin repeat
Structure domains: Severin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Gelsolin: the tail of a molecular gymnast.
Nag et al. (2013)
5 more

4 mentions without citation

Improved prediction of critical residues for protein function based on network and phylogenetic analyses.
Thibert et al. (2005)
3 more