Structure analysis

X-RAY SIRAS STRUCTURE DETERMINATION OF A VANADIUM-DEPENDENT HALOPEROXIDASE FROM ASCOPHYLLUM NODOSUM AT 2.0 A RESOLUTION

X-ray diffraction
2.05Å resolution
Source organism: Ascophyllum nodosum
Assembly composition:
hetero dimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
Download    3D Visualisation
Multimeric state: hetero dimer
Accessible surface area: 34596.16 Å2
Buried surface area: 11102.43 Å2
Dissociation area: 5,332.17 Å2
Dissociation energy (ΔGdiss): 72.36 kcal/mol
Dissociation entropy (TΔSdiss): 15.93 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-223924

Macromolecules

Chain: A
Length: 556 amino acids
Theoretical weight: 60.66 KDa
Source organism: Ascophyllum nodosum
UniProt:
  • Canonical: P81701 (Residues: 1-556; Coverage: 100%)
InterPro:
CATH: Vanadium-containing Chloroperoxidase, domain 2
SCOP: Haloperoxidase (bromoperoxidase)

Search similar proteins

Chain: B
Length: 556 amino acids
Theoretical weight: 60.54 KDa
Source organism: Ascophyllum nodosum
UniProt:
  • Canonical: P81701 (Residues: 1-556; Coverage: 100%)
InterPro:
CATH: Vanadium-containing Chloroperoxidase, domain 2
SCOP: Haloperoxidase (bromoperoxidase)

Search similar proteins