› 3emn

X-ray diffraction
2.3Å resolution

The Crystal Structure of Mouse VDAC1 at 2.3 A resolution

Released:
DOI: 10.2210/pdb3emn/pdb
PDB entry 3emn coloured by chain, front view.
PDB entry 3emn coloured by chain, side view.
PDB entry 3emn coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
The crystal structure of mouse VDAC1 at 2.3 A resolution reveals mechanistic insights into metabolite gating.
Ujwal R, Cascio D, Colletier JP, Faham S, Zhang J, Toro L, Ping P, Abramson J
Proc Natl Acad Sci U S A 105 17742-7 (2008)
PMID: 18988731

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-178829 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Voltage-dependent anion-selective channel protein 1 Chain: X
Molecule details ›
Chain: X
Length: 295 amino acids
Theoretical weight: 32.2 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q60932 (Residues: 14-296; Coverage: 96%)
Gene names: Vdac1, Vdac5
Sequence domains: Eukaryotic porin
Structure domains: Porin

Ligands and Environments

1 bound ligand:
Ligand MC3 1 x MC3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E, ALS BEAMLINE 5.0.2
Spacegroup: C2
Unit cell:
a: 100.23Å b: 58.39Å c: 66.58Å
α: 90° β: 99.25° γ: 90°
R-values:
R R work R free
0.244 0.242 0.277
Expression system: Escherichia coli

Quick links

Citations

82 review citations

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

89 mentions without citation

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