A Role for Active Site Water Molecules and Hydroxyl Groups of Substrate for Oxygen Activation in Cytochrome P450 158A2

Summary for 2D09

Related1T93 1SE6 1S1F
Descriptorputative cytochrome P450, PROTOPORPHYRIN IX CONTAINING FE, FLAVIOLIN, ... (5 entities in total)
Functional Keywordsstreptomyces, cytochrome p450 oxidoreductase, cyp158a2, proton transfer, dioxygen activation, oxidoreductase
Biological sourceStreptomyces coelicolor
Total number of polymer chains1
Total molecular weight45682.52
Zhao, B.,Waterman, M.R. (deposition date: 2005-07-30, release date: 2005-10-25, Last modification date: 2017-10-11)
Primary citation
Zhao, B.,Guengerich, F.P.,Voehler, M.,Waterman, M.R.
Role of active site water molecules and substrate hydroxyl groups in oxygen activation by cytochrome P450 158A2: a new mechanism of proton transfer
J.Biol.Chem., 280:42188-42197, 2005
PubMed: 16239228 (PDB entries with the same primary citation)
DOI: 10.1074/jbc.M509220200
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.251233.2%6.7%8.7%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload
PDB entries from 2020-08-12