› 5l0c

X-ray diffraction
3.1Å resolution

Human metavinculin (residues 959-1134) in complex with PIP2

Released:
DOI: 10.2210/pdb5l0c/pdb
PDB entry 5l0c coloured by chain, front view.
PDB entry 5l0c coloured by chain, side view.
PDB entry 5l0c 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: 176 amino acids
Theoretical weight: 19.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P18206 (Residues: 959-1134; Coverage: 16%)
Gene name: VCL
Sequence domains: Vinculin family
Structure domains: Alpha-catenin/vinculin-like

Ligands and Environments

2 bound ligands:
Ligand PIO 5 x PIO
Ligand PO4 3 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: C2
Unit cell:
a: 114.52Å b: 100.676Å c: 105.615Å
α: 90° β: 122.49° γ: 90°
R-values:
R R work R free
0.237 0.235 0.261
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

1 mention without citation

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