› 2k4t

Solution NMR

Solution structure of human VDAC-1 in LDAO micelles

Released:
DOI: 10.2210/pdb2k4t/pdb
PDB entry 2k4t coloured by chain, ensemble of 20 models, front view.
PDB entry 2k4t coloured by chain, ensemble of 20 models, side view.
PDB entry 2k4t coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of the integral human membrane protein VDAC-1 in detergent micelles.
Hiller S, Garces RG, Malia TJ, Orekhov VY, Colombini M, Wagner G
Science 321 1206-10 (2008)
PMID: 18755977

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149424 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Voltage-dependent anion-selective channel protein 1 Chain: A
Molecule details ›
Chain: A
Length: 291 amino acids
Theoretical weight: 31.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P21796 (Residues: 1-283; Coverage: 100%)
Gene names: VDAC, VDAC1
Sequence domains: Eukaryotic porin
Structure domains: Porin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

122 review citations

VDAC, a multi-functional mitochondrial protein regulating cell life and death.
Shoshan-Barmatz et al. (2010)
121 more

38 mentions without citation

The structural biology of β-barrel membrane proteins: a summary of recent reports.
Fairman et al. (2011)
37 more