› 5l0d

X-ray diffraction
2.75Å resolution

Human Metavinculin(residues 959-1130) in complex with PIP2

Released:
DOI: 10.2210/pdb5l0d/pdb
PDB entry 5l0d coloured by chain, front view.
PDB entry 5l0d coloured by chain, side view.
PDB entry 5l0d coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Differential lipid binding of vinculin isoforms promotes quasi-equivalent dimerization.
Chinthalapudi K, Rangarajan ES, Brown DT, Izard T
Proc Natl Acad Sci U S A 113 9539-44 (2016)
PMID: 27503891

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148327 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vinculin Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 172 amino acids
Theoretical weight: 19.05 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P18206 (Residues: 959-1130; Coverage: 15%)
Gene name: VCL
Sequence domains: Vinculin family
Structure domains: Alpha-catenin/vinculin-like

Ligands and Environments

1 bound ligand:
Ligand PIO 3 x PIO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C2
Unit cell:
a: 120.617Å b: 58.55Å c: 112.492Å
α: 90° β: 113.15° γ: 90°
R-values:
R R work R free
0.209 0.207 0.259
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Roles of Membrane Domains in Integrin-Mediated Cell Adhesion.
Lietha et al. (2020)
1 more

2 mentions without citation

Differential lipid binding of vinculin isoforms promotes quasi-equivalent dimerization.
Chinthalapudi et al. (2016)
1 more