› 5iki

X-ray diffraction
2.4Å resolution

CYP106A2 WITH SUBSTRATE ABIETIC ACID

Released:
DOI: 10.2210/pdb5iki/pdb
PDB entry 5iki coloured by chain, front view.
PDB entry 5iki coloured by chain, side view.
PDB entry 5iki coloured by chain, top view.
Source organism: Priestia megaterium
Primary publication:
Crystal Structure of CYP106A2 in Substrate-Free and Substrate-Bound Form.
Janocha S, Carius Y, Hutter M, Lancaster CR, Bernhardt R
Chembiochem 17 852-60 (2016)
PMID: 26864272

Function and Biology Details

Reaction catalysed: 
Progesterone + 2 reduced [2Fe-2S] ferredoxin + O(2) = 15-beta-hydroxyprogesterone + 2 oxidized [2Fe-2S] ferredoxin + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170282 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome P450(MEG) Chains: A, B
Molecule details ›
Chains: A, B
Length: 410 amino acids
Theoretical weight: 47.02 KDa
Source organism: Priestia megaterium
Expression system: Escherichia coli
UniProt:
  • Canonical: Q06069 (Residues: 1-410; Coverage: 100%)
Gene name: cyp106A2
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
1 bound ligand:
Ligand A9H 1 x A9H
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P1
Unit cell:
a: 48.91Å b: 57.39Å c: 84.24Å
α: 72.37° β: 75.19° γ: 75.7°
R-values:
R R work R free
0.204 0.201 0.261
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Engineering cytochrome P450 enzyme systems for biomedical and biotechnological applications.
Li et al. (2020)
1 more

2 mentions without citation

Binding modes of CYP106A2 redox partners determine differences in progesterone hydroxylation product patterns.
Sagadin et al. (2018)
1 more