› 5xdn

X-ray diffraction
3.15Å resolution

Crystal structure of human voltage-dependent anion channel 1 (hVDAC1) in P22121 space group

Released:
DOI: 10.2210/pdb5xdn/pdb
PDB entry 5xdn coloured by chain, front view.
PDB entry 5xdn coloured by chain, side view.
PDB entry 5xdn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structural characterization reveals novel oligomeric interactions of human voltage-dependent anion channel 1.
Hosaka T, Okazaki M, Kimura-Someya T, Ishizuka-Katsura Y, Ito K, Yokoyama S, Dodo K, Sodeoka M, Shirouzu M
Protein Sci 26 1749-1758 (2017)
PMID: 28608415

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149425 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Voltage-dependent anion-selective channel protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 295 amino acids
Theoretical weight: 32.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P21796 (Residues: 1-283; Coverage: 100%)
Gene names: VDAC, VDAC1
Sequence domains: Eukaryotic porin
Structure domains: Porin

Ligands and Environments

4 bound ligands:
Ligand D12 2 x D12
Ligand HEX 4 x HEX
Ligand OCT 1 x OCT
Ligand D10 2 x D10
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL32XU
Unit cell:
a: 58.7Å b: 84.96Å c: 146.23Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.267 0.266 0.3
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Contribution of Mitochondrial Ion Channels to Chemo-Resistance in Cancer Cells.
Peruzzo et al. (2019)
1 more

5 mentions without citation

VDAC1 as Pharmacological Target in Cancer and Neurodegeneration: Focus on Its Role in Apoptosis.
Magrì et al. (2018)
4 more