› 1p3u

X-ray diffraction
1.75Å resolution

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

Released:
DOI: 10.2210/pdb1p3u/pdb
PDB entry 1p3u coloured by chain, front view.
PDB entry 1p3u coloured by chain, side view.
PDB entry 1p3u 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 NO 1 x NO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P43212
Unit cell:
a: 63.033Å b: 63.033Å c: 101.105Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.252 0.252 0.287
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