› 1ged

X-ray diffraction
2Å resolution

A positive charge route for the access of nadh to heme formed in the distal heme pocket of cytochrome p450nor

Released:
DOI: 10.2210/pdb1ged/pdb
PDB entry 1ged coloured by chain, front view.
PDB entry 1ged coloured by chain, side view.
PDB entry 1ged coloured by chain, top view.
Source organism: Fusarium oxysporum
Primary publication:
A positively charged cluster formed in the heme-distal pocket of cytochrome P450nor is essential for interaction with NADH.
Kudo T, Takaya N, Park SY, Shiro Y, Shoun H
J Biol Chem 276 5020-6 (2001)
PMID: 11076941

Function and Biology Details

Reaction catalysed: 
Nitrous oxide + NAD(P)(+) + H(2)O = 2 nitric oxide + NAD(P)H
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-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: 44.42 KDa
Source organism: Fusarium oxysporum
Expression system: Escherichia coli
UniProt:
  • Canonical: P23295 (Residues: 1-403; Coverage: 100%)
Gene names: CYP55, CYP55A1
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
1 bound ligand:
Ligand BR 2 x BR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: P212121
Unit cell:
a: 54.32Å b: 78.05Å c: 86.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.214 0.279
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Fungal denitrification and nitric oxide reductase cytochrome P450nor.
Shoun et al. (2012)
4 more