1wov

X-ray diffraction
1.75Å resolution

Crystal structure of heme oxygenase-2 from Synechocystis sp. PCC 6803 in complex with heme

Released:

Function and Biology Details

Reaction catalysed:
Protoheme + 3 [reduced NADPH--hemoprotein reductase] + 3 O(2) = biliverdin + Fe(2+) + CO + 3 [oxidized NADPH--hemoprotein reductase] + 3 H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159928 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heme oxygenase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 250 amino acids
Theoretical weight: 28.57 KDa
Source organism: Synechocystis sp. PCC 6803
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P74133 (Residues: 1-250; Coverage: 100%)
Gene names: pbsA2, sll1875
Sequence domains: Heme oxygenase
Structure domains: Heme oxygenase-like

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P21
Unit cell:
a: 58.163Å b: 74.585Å c: 72.661Å
α: 90° β: 108.15° γ: 90°
R-values:
R R work R free
0.198 0.193 0.254
Expression system: Escherichia coli BL21(DE3)