2dkk

X-ray diffraction
1.97Å resolution

Structure/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:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-192179 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Biflaviolin synthase CYP158A1 Chain: A
Molecule details ›
Chain: A
Length: 411 amino acids
Theoretical weight: 45.31 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: 103.968Å b: 44.352Å c: 102.107Å
α: 90° β: 114.44° γ: 90°
R-values:
R R work R free
0.244 0.228 0.285
Expression system: Escherichia coli BL21(DE3)