› 4wmh

X-ray diffraction
2.5Å resolution

Structure of heme oxygenase-2 containing residues 1-288 lacking the membrane spanning region

Released:
DOI: 10.2210/pdb4wmh/pdb
PDB entry 4wmh coloured by chain, front view.
PDB entry 4wmh coloured by chain, side view.
PDB entry 4wmh coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Bianchetti CM, Li Y, Ragsdale SW, Phillips Jr GN, Center for Eukaryotic Structural Genomics (CESG)

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151751 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heme oxygenase 2 soluble form Chain: A
Molecule details ›
Chain: A
Length: 207 amino acids
Theoretical weight: 24.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P30519 (Residues: 31-237; Coverage: 66%)
Gene names: HMOX2, HO2
Sequence domains: Heme oxygenase
Structure domains: Heme oxygenase-like

Ligands and Environments

1 bound ligand:
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P4322
Unit cell:
a: 35.69Å b: 35.69Å c: 366.706Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.231 0.226 0.27
Expression system: Escherichia coli BL21(DE3)

Quick links