› 1dvg

X-ray diffraction
2.2Å resolution

CRYSTAL STRUCTURE OF RAT HEME OXYGENASE-1 IN COMPLEX WITH HEME; SELELENO-METHIONINE DERIVATIVE, MUTATED AT M51T,M93L,M155L,M191L.

Released:
DOI: 10.2210/pdb1dvg/pdb
PDB entry 1dvg coloured by chain, front view.
PDB entry 1dvg coloured by chain, side view.
PDB entry 1dvg coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Crystal structure of rat heme oxygenase-1 in complex with heme.
Sugishima M, Omata Y, Kakuta Y, Sakamoto H, Noguchi M, Fukuyama K
FEBS Lett 471 61-6 (2000)
PMID: 10760513

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:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139216 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heme oxygenase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 267 amino acids
Theoretical weight: 30.66 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P06762 (Residues: 1-267; Coverage: 92%)
Gene name: Hmox1
Sequence domains: Heme oxygenase
Structure domains: Heme oxygenase-like

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
No bound ligands
1 modified residue:
Ligand MSE 8 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P43
Unit cell:
a: 54.853Å b: 54.853Å c: 187.558Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.212 0.258
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Heme enzyme structure and function.
Poulos TL. (2014)
13 more

1 mention without citation

Transthyretin Mimetics as Anti-β-Amyloid Agents: A Comparison of Peptide and Protein Approaches.
Pate et al. (2018)