› 6tir

Solution NMR

NOE based model of hVDAC-1 bound to beta-NADH in detergent micelles

Released:
DOI: 10.2210/pdb6tir/pdb
PDB entry 6tir coloured by chain, ensemble of 10 models, front view.
PDB entry 6tir coloured by chain, ensemble of 10 models, side view.
PDB entry 6tir coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
The Structural Basis for Low Conductance in the Membrane Protein VDAC upon β-NADH Binding and Voltage Gating.
Böhm R, Amodeo GF, Murlidaran S, Chavali S, Wagner G, Winterhalter M, Brannigan G, Hiller S
Structure 28 206-214.e4 (2020)
PMID: 31862297

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:
Non-selective voltage-gated ion channel VDAC1 Chain: A
Molecule details ›
Chain: A
Length: 291 amino acids
Theoretical weight: 31.88 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

Ligands and Environments

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

Experiments and Validation Details

wwPDB Validation report is not available for this NMR entry.
Chemical shift assignment: 40%
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

5 review citations

A Calcium Guard in the Outer Membrane: Is VDAC a Regulated Gatekeeper of Mitochondrial Calcium Uptake?
Sander et al. (2021)
4 more

4 mentions without citation

The Role of Voltage-Dependent Anion Channel in Mitochondrial Dysfunction and Human Disease.
Varughese et al. (2021)
3 more