› 4c69

X-ray diffraction
2.28Å resolution

ATP binding to murine voltage-dependent anion channel 1 (mVDAC1).

Released:
DOI: 10.2210/pdb4c69/pdb
PDB entry 4c69 coloured by chain, front view.
PDB entry 4c69 coloured by chain, side view.
PDB entry 4c69 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structure-guided simulations illuminate the mechanism of ATP transport through VDAC1.
Choudhary OP, Paz A, Adelman JL, Colletier JP, Abramson J, Grabe M
Nat Struct Mol Biol 21 626-32 (2014)
PMID: 24908397

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-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 M15
UniProt:
  • Canonical: Q60932 (Residues: 14-296; Coverage: 96%)
Gene names: Vdac1, Vdac5
Sequence domains: Eukaryotic porin
Structure domains: Porin

Ligands and Environments

3 bound ligands:
Ligand LDA 6 x LDA
Ligand MC3 2 x MC3
Ligand ATP 1 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: C2
Unit cell:
a: 100.152Å b: 58.369Å c: 66.545Å
α: 90° β: 99.25° γ: 90°
R-values:
R R work R free
0.207 0.204 0.261
Expression system: Escherichia coli M15

Quick links

Citations

14 review citations

Mitochondrial VDAC1: A Key Gatekeeper as Potential Therapeutic Target.
Camara et al. (2017)
13 more

10 mentions without citation

Ten Years of High Resolution Structural Research on the Voltage Dependent Anion Channel (VDAC)-Recent Developments and Future Directions.
Zeth et al. (2018)
9 more