6tiq

Solution NMR

Refined solution NMR structure of hVDAC-1 in detergent micelles

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Voltage-dependent anion-selective channel protein 1 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

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 40%
Refinement method: torsion angle dynamics
Chemical shifts: BMR34457  
Expression system: Escherichia coli