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Structure paper

TitleEnzyme-substrate complex structures of CYP154C5 shed light on its mode of highly selective steroid hydroxylation.
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 70, Page 2875-2889, Year 2014
Publish dateFeb 11, 2013 (structure data deposition date)
AuthorsHerzog, K. / Bracco, P. / Onoda, A. / Hayashi, T. / Hoffmann, K. / Schallmey, A.
External linksActa Crystallogr. ,Sect. D / PubMed:25372679
MethodsX-ray diffraction
Resolution1.9 - 2.4 Å
Structure data

PDB-4j6b:
The 2.2 A crystal structure of CYP154C5 from Nocardia farcinica in complex with pregnenolone
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-4j6c:
The 1.9 A crystal structure of CYP154C5 from Nocardia farcinica in complex with progesterone
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-4j6d:
The 2.4 A crystal structure of CYP154C5 from Nocardia farcinica in complex with testosterone
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-4jbt:
The 2.2 A crystal structure of CYP154C5 from Nocardia farcinica in complex with androstenedione
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-PLO:
(3BETA)-3-HYDROXYPREGN-5-EN-20-ONE / medication, hormone*YM

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-MG:
Unknown entry

ChemComp-FMT:
FORMIC ACID

ChemComp-K:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-STR:
PROGESTERONE / hormone*YM

ChemComp-TES:
TESTOSTERONE / hormone*YM

ChemComp-ASD:
4-ANDROSTENE-3-17-DIONE / hormone*YM

Source
  • nocardia farcinica (bacteria)
Keywordsoxidoreductase/substrate / Cytochrom P450 / steroid hydroxylating monooxygenase / steroid binding / oxidoreductase-substrate complex

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