› 4ap3

X-ray diffraction
2.39Å resolution

Oxidized steroid monooxygenase bound to NADP

Released:
DOI: 10.2210/pdb4ap3/pdb
PDB entry 4ap3 coloured by chain, front view.
PDB entry 4ap3 coloured by chain, side view.
PDB entry 4ap3 coloured by chain, top view.
Source organism: Rhodococcus rhodochrous
Primary publication:
Exploring the structural basis of substrate preferences in Baeyer-Villiger monooxygenases: insight from steroid monooxygenase.
Franceschini S, van Beek HL, Pennetta A, Martinoli C, Fraaije MW, Mattevi A
J Biol Chem 287 22626-34 (2012)
PMID: 22605340

Function and Biology Details

Reaction catalysed: 
17-alpha-hydroxyprogesterone + NADPH + O(2) = androstenedione + NADP(+) + H(2)O + acetate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129332 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Steroid monooxygenase Chain: A
Molecule details ›
Chain: A
Length: 549 amino acids
Theoretical weight: 60.21 KDa
Source organism: Rhodococcus rhodochrous
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O50641 (Residues: 1-549; Coverage: 100%)
Sequence domains: Flavin-binding monooxygenase-like
Structure domains: FAD/NAD(P)-binding domain

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD

Cofactor: Ligand NAP 1 x NAP
1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P41212
Unit cell:
a: 81.75Å b: 81.75Å c: 228.07Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.207 0.239
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Flavoprotein monooxygenases for oxidative biocatalysis: recombinant expression in microbial hosts and applications.
Ceccoli et al. (2014)
2 more

1 mention without citation

Exploring the structural basis of substrate preferences in Baeyer-Villiger monooxygenases: insight from steroid monooxygenase.
Franceschini et al. (2012)