2nz5

X-ray diffraction
2.35Å resolution

Structure and Function Studies of Cytochrome P450 158A1 from Streptomyces coelicolor A3(2)

Released:

Function and Biology Details

Reaction catalysed:
2 flaviolin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+) + O(2) = 3,3'-biflaviolin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-192180 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Biflaviolin synthase CYP158A1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 413 amino acids
Theoretical weight: 45.59 KDa
Source organism: Streptomyces coelicolor A3(2)
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9KZF5 (Residues: 1-407; Coverage: 100%)
Gene names: SCO6998, cyp158a1
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: C2
Unit cell:
a: 192.267Å b: 44.859Å c: 105.052Å
α: 90° β: 97.76° γ: 90°
R-values:
R R work R free
0.252 0.235 0.293
Expression system: Escherichia coli BL21(DE3)