› 1ydi

X-ray diffraction
1.8Å resolution

Human Vinculin Head Domain (VH1, 1-258) in Complex with Human Alpha-Actinin's Vinculin-Binding Site (Residues 731-760)

Released:
DOI: 10.2210/pdb1ydi/pdb
PDB entry 1ydi coloured by chain, front view.
PDB entry 1ydi coloured by chain, side view.
PDB entry 1ydi coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural dynamics of alpha-actinin-vinculin interactions.
Bois PR, Borgon RA, Vonrhein C, Izard T
Mol Cell Biol 25 6112-22 (2005)
PMID: 15988023

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129067 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Vinculin Chain: A
Molecule details ›
Chain: A
Length: 263 amino acids
Theoretical weight: 29.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P18206 (Residues: 1-258; Coverage: 23%)
Gene name: VCL
Sequence domains: Vinculin family
Structure domains: Alpha-catenin/vinculin-like
Alpha-actinin-4 Chain: B
Molecule details ›
Chain: B
Length: 24 amino acids
Theoretical weight: 2.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O43707 (Residues: 734-757; Coverage: 3%)
Gene name: ACTN4

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 42.843Å b: 54.268Å c: 63.598Å
α: 90° β: 107.57° γ: 90°
R-values:
R R work R free
0.181 0.171 0.232
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Regulation of actin assembly associated with protrusion and adhesion in cell migration.
Le Clainche et al. (2008)
11 more

6 mentions without citation

Structural dynamics of alpha-actinin-vinculin interactions.
Bois et al. (2005)
5 more