› 5jdp

Solution NMR

E73V mutant of the human voltage-dependent anion channel

Released:
DOI: 10.2210/pdb5jdp/pdb
PDB entry 5jdp coloured by chain, ensemble of 20 models, front view.
PDB entry 5jdp coloured by chain, ensemble of 20 models, side view.
PDB entry 5jdp coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
High-Resolution NMR Determination of the Dynamic Structure of Membrane Proteins.
Jaremko M, Jaremko Ł, Villinger S, Schmidt CD, Griesinger C, Becker S, Zweckstetter M
Angew Chem Int Ed Engl 55 10518-21 (2016)
PMID: 27461260

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: 285 amino acids
Theoretical weight: 30.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P21796 (Residues: 2-283; 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
Chemical shift assignment: 27%
Expression system: Escherichia coli

Quick links

Citations

5 review citations

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

6 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)
5 more