› 3myi

X-ray diffraction
2.2Å resolution

Human metavinculin tail domain

Released:
DOI: 10.2210/pdb3myi/pdb
PDB entry 3myi coloured by chain, front view.
PDB entry 3myi coloured by chain, side view.
PDB entry 3myi coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A helix replacement mechanism directs metavinculin functions.
Rangarajan ES, Lee JH, Yogesha SD, Izard T
PLoS One 5 e10679 (2010)
PMID: 20502710

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148317 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vinculin Chain: A
Molecule details ›
Chain: A
Length: 172 amino acids
Theoretical weight: 19.05 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P18206 (Residues: 959-1130; Coverage: 15%)
Gene name: VCL
Sequence domains: Vinculin family
Structure domains: Alpha-catenin/vinculin-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Unit cell:
a: 62.443Å b: 62.443Å c: 62.443Å
α: 111.87° β: 111.87° γ: 111.87°
R-values:
R R work R free
0.193 0.19 0.247
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Vinculin and metavinculin: oligomerization and interactions with F-actin.
Thompson et al. (2013)
1 more

7 mentions without citation

Updates to the Integrated Protein-Protein Interaction Benchmarks: Docking Benchmark Version 5 and Affinity Benchmark Version 2.
Vreven et al. (2015)
6 more