1we1

X-ray diffraction
2.5Å resolution

Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC6803 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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159866 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heme oxygenase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 240 amino acids
Theoretical weight: 27.08 KDa
Source organism: Synechocystis sp. PCC 6803
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P72849 (Residues: 1-240; Coverage: 100%)
Gene names: pbsA1, sll1184
Sequence domains: Heme oxygenase
Structure domains: Heme oxygenase-like

Ligands and Environments


Cofactor: Ligand HEM 4 x HEM
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: C2
Unit cell:
a: 110.79Å b: 113.73Å c: 109.7Å
α: 90° β: 112.26° γ: 90°
R-values:
R R work R free
0.224 0.22 0.269
Expression system: Escherichia coli BL21(DE3)