Structure analysis

Crystal structure of human voltage-dependent anion channel 1 (hVDAC1) in C222 space group

X-ray diffraction
3.1Å resolution
Source organism: Homo sapiens
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 32342.52 Å2
Buried surface area: 3328.79 Å2
Dissociation area: 599.97 Å2
Dissociation energy (ΔGdiss): -28.6 kcal/mol
Dissociation entropy (TΔSdiss): 13.24 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-149425

Macromolecules

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
Pfam: Eukaryotic porin
InterPro:
CATH: Porin
PDBe-KB: UniProt Coverage View: P21796  
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