Structure analysis

Crystal structure of Vanadium-dependent Haloperoxidase from A. marina

X-ray diffraction
3.1Å resolution
Source organism: Acaryochloris marina
Assembly composition:
homo dodecamer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dodecamer
Accessible surface area: 99500 Å2
Buried surface area: 14300 Å2
Dissociation area: 300 Å2
Dissociation energy (ΔGdiss): -11 kcal/mol
Dissociation entropy (TΔSdiss): 14 kcal/mol
Interface energy (ΔGint): -69 kcal/mol
Symmetry number: 1

Macromolecules

Chain: A
Length: 666 amino acids
Theoretical weight: 73.07 KDa
Source organism: Acaryochloris marina
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B0C4R0 (Residues: 1-639; Coverage: 100%)
Gene name: AM1_4975
InterPro:
CATH: Vanadium-containing Chloroperoxidase, domain 2

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