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Crystal structure of Vanadium-dependent Haloperoxidase from A. marina

X-ray diffraction
3.1Å resolution
PDB 5lpc coloured by chain and viewed from the front.
PDB 5lpc coloured by chain and viewed from the side.
PDB 5lpc coloured by chain and viewed from the top.
Source organism: Acaryochloris marina
Assembly composition:
homo dodecamer (preferred)
Entry contents: 1 distinct polypeptide molecule

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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

Vanadium-dependent bromoperoxidase, putative
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
PDB 5lpc contains 12 copies of Vanadium-dependent bromoperoxidase, putative in assembly 1. This protein is highlighted and viewed from the front.
PDB 5lpc contains 12 copies of Vanadium-dependent bromoperoxidase, putative in assembly 1. This protein is highlighted and viewed from the side.
PDB 5lpc contains 12 copies of Vanadium-dependent bromoperoxidase, putative in assembly 1. This protein is highlighted and viewed from the top.
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