› 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:
DOI: 10.2210/pdb1p3v/pdb
PDB entry 1p3v coloured by chain, front view.
PDB entry 1p3v coloured by chain, side view.
PDB entry 1p3v coloured by chain, top view.
Source organism: Neisseria meningitidis
Primary publication:
Crystal structures of the NO- and CO-bound heme oxygenase from Neisseriae meningitidis. Implications for O2 activation.
Friedman J, Lad L, Deshmukh R, Li H, Wilks A, Poulos TL
J Biol Chem 278 34654-9 (2003)
PMID: 12819228

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193167 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
HemO 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:
Ligand HEM 1 x HEM
Ligand CMO 1 x CMO
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)

Quick links

Citations

4 review citations

Heme and virulence: how bacterial pathogens regulate, transport and utilize heme.
Wilks et al. (2007)
3 more

1 mention without citation

Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis. A 1H NMR study.
Peng et al. (2011)