5HIW
Sorangium cellulosum So Ce56 cytochrome P450 260B1
Summary for 5HIW
| Entry DOI | 10.2210/pdb5hiw/pdb |
| Descriptor | Cytochrome P450 CYP260B1, PROTOPORPHYRIN IX CONTAINING FE, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | p450, cytochrome, cyp, sorangium, 260b1, steroids, oxidoreductase |
| Biological source | Sorangium cellulosum (strain So ce56) |
| Total number of polymer chains | 1 |
| Total formula weight | 44211.78 |
| Authors | Salamanca-Pinzon, S.G.,Carius, Y.,Khatri, Y.,Bernhardt, R.,Lancaster, C.R.D. (deposition date: 2016-01-12, release date: 2016-08-03, Last modification date: 2024-01-10) |
| Primary citation | Salamanca-Pinzon, S.G.,Khatri, Y.,Carius, Y.,Keller, L.,Muller, R.,Lancaster, C.R.,Bernhardt, R. Structure-function analysis for the hydroxylation of Delta 4 C21-steroids by the myxobacterial CYP260B1. Febs Lett., 590:1838-1851, 2016 Cited by PubMed Abstract: Myxobacterial CYP260B1 from Sorangium cellulosum was heterologously expressed in Escherichia coli and purified. The in vitro conversion of a small focused substrate library comprised of Δ4 C21-steroids and steroidal drugs using surrogate bovine redox partners shows that CYP260B1 is a novel steroid hydroxylase. CYP260B1 performs the regio- and stereoselective hydroxylation of the glucocorticoid cortodoxone (RSS) to produce 6β-OH-RSS. The substrate-free crystal structure of CYP260B1 (PDB 5HIW) was resolved. Docking of the tested ligands into the crystal structure suggested that the C17 hydroxy moiety and the presence of either a keto or a hydroxy group at C11 determine the selectivity of hydroxylation. PubMed: 27177597DOI: 10.1002/1873-3468.12217 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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