› 3dbg

X-ray diffraction
2.6Å resolution

Crystal structure of Cytochrome P450 170A1 (CYP170A1) from Streptomyces coelicolor

Released:
DOI: 10.2210/pdb3dbg/pdb
PDB entry 3dbg coloured by chain, front view.
PDB entry 3dbg coloured by chain, side view.
PDB entry 3dbg coloured by chain, top view.
Source organism: Streptomyces coelicolor A3(2)
Primary publication:
Crystal structure of albaflavenone monooxygenase containing a moonlighting terpene synthase active site.
Zhao B, Lei L, Vassylyev DG, Lin X, Cane DE, Kelly SL, Yuan H, Lamb DC, Waterman MR
J Biol Chem 284 36711-36719 (2009)
PMID: 19858213

Function and Biology Details

Reactions catalysed: 
(+)-epi-isozizaene + 4 reduced [2Fe-2S] ferredoxin + 4 H(+) + 2 O(2) = albaflavenone + 4 oxidized [2Fe-2S] ferredoxin + 3 H(2)O
(2E,6E)-farnesyl diphosphate = (E)-beta-farnesene + diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191757 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional albaflavenone monooxygenase/terpene synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 467 amino acids
Theoretical weight: 51.84 KDa
Source organism: Streptomyces coelicolor A3(2)
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9K498 (Residues: 1-461; Coverage: 100%)
Gene name: SCO5223
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P63
Unit cell:
a: 103.596Å b: 103.596Å c: 140.861Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.212 0.208 0.23
Expression system: Escherichia coli

Quick links

Citations

19 review citations

Unusual cytochrome p450 enzymes and reactions.
Guengerich et al. (2013)
18 more

13 mentions without citation

Conformational plasticity and structure/function relationships in cytochromes P450.
Pochapsky et al. (2010)
12 more