6fu3

X-ray diffraction
1.8Å resolution

Structure of the mixed-valence, active form, of cytochrome c peroxidase from obligate human pathogenic bacterium Neisseria gonorrhoeae

Released:
Model geometry
Fit model/data
Source organism: Neisseria gonorrhoeae
Entry authors: Carvalho AL, Romao MJ, Pauleta S, Nobrega C

Function and Biology Details

Reaction catalysed:
2 ferrocytochrome c + H(2)O(2) = 2 ferricytochrome c + 2 H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-177058 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome c domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 339 amino acids
Theoretical weight: 37.62 KDa
Source organism: Neisseria gonorrhoeae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5F5Z9 (Residues: 59-387; Coverage: 89%)
Gene name: NGO_1769
Sequence domains:
Structure domains: Cytochrome c-like domain

Ligands and Environments


Cofactor: Ligand HEC 4 x HEC
1 bound ligand:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: BRUKER IMUS MICROFOCUS
Spacegroup: P212121
Unit cell:
a: 78.942Å b: 88.78Å c: 93.122Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.208 0.244
Expression system: Escherichia coli