› 1twn

X-ray diffraction
2.2Å resolution

Crystal structures of ferrous and ferrous-NO forms of verdoheme in a complex with human heme oxygenase-1: catalytic implications for heme cleavage

Released:
DOI: 10.2210/pdb1twn/pdb
PDB entry 1twn coloured by chain, front view.
PDB entry 1twn coloured by chain, side view.
PDB entry 1twn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of ferrous and ferrous-NO forms of verdoheme in a complex with human heme oxygenase-1: catalytic implications for heme cleavage.
Lad L, Ortiz de Montellano PR, Poulos TL
J Inorg Biochem 98 1686-95 (2004)
PMID: 15522396

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
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140706 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heme oxygenase 1 soluble form Chains: A, B
Molecule details ›
Chains: A, B
Length: 233 amino acids
Theoretical weight: 26.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09601 (Residues: 1-233; Coverage: 81%)
Gene names: HMOX1, HO, HO1
Sequence domains: Heme oxygenase
Structure domains: Heme oxygenase-like

Ligands and Environments

1 bound ligand:
Ligand VER 2 x VER
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21
Unit cell:
a: 61.607Å b: 54.562Å c: 71.72Å
α: 90° β: 99.24° γ: 90°
R-values:
R R work R free
0.196 not available not available
Expression system: Escherichia coli

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Citations

4 review citations

Structure and catalytic mechanism of heme oxygenase.
Unno et al. (2007)
3 more