1p3v

X-ray diffraction
2.25Å resolution

Crystal Structures of the NO-and CO-Bound Heme Oxygenase From Neisseria Meningitidis: Implications for Oxygen Activation

Released:

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heme utilization protein Chain: A
Molecule details ›
Chain: A
Length: 209 amino acids
Theoretical weight: 23.61 KDa
Source organism: Neisseria meningitidis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9RGD9 (Residues: 22-230; Coverage: 91%)
Gene names: NMA510612_2169, hemO
Sequence domains: Heme oxygenase
Structure domains: Heme oxygenase-like

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P43212
Unit cell:
a: 60.449Å b: 60.449Å c: 102.361Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.249 0.249 0.286
Expression system: Escherichia coli BL21(DE3)