› 1ehg

X-ray diffraction
1.7Å resolution

CRYSTAL STRUCTURES OF CYTOCHROME P450NOR AND ITS MUTANTS (SER286 VAL, THR) IN THE FERRIC RESTING STATE AT CRYOGENIC TEMPERATURE: A COMPARATIVE ANALYSIS WITH MONOOXYGENASE CYTOCHROME P450S

Released:
DOI: 10.2210/pdb1ehg/pdb
PDB entry 1ehg coloured by chain, front view.
PDB entry 1ehg coloured by chain, side view.
PDB entry 1ehg coloured by chain, top view.
Source organism: Fusarium oxysporum
Primary publication:
Crystal structures of cytochrome P450nor and its mutants (Ser286-->Val, Thr) in the ferric resting state at cryogenic temperature: a comparative analysis with monooxygenase cytochrome P450s.
Shimizu H, Park S, Lee D, Shoun H, Shiro Y
J Inorg Biochem 81 191-205 (2000)
PMID: 11051564

Function and Biology Details

Reaction catalysed: 
Nitrous oxide + NAD(P)(+) + H(2)O = 2 nitric oxide + NAD(P)H
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149924 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NADP nitrous oxide-forming nitric oxide reductase Chain: A
Molecule details ›
Chain: A
Length: 403 amino acids
Theoretical weight: 44.43 KDa
Source organism: Fusarium oxysporum
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: P23295 (Residues: 2-403; Coverage: 100%)
Gene names: CYP55, CYP55A1
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: P212121
Unit cell:
a: 54.751Å b: 81.86Å c: 85.72Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.193 0.223
Expression system: Escherichia coli K-12

Quick links

Citations

4 review citations

Functional interaction of cytochrome P450 with its redox partners: a critical assessment and update of the topology of predicted contact regions.
Hlavica et al. (2003)
3 more