This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1oxa
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1oxa |SIZE=350|CAPTION= <scene name='initialview01'>1oxa</scene>, resolution 2.1Å | |PDB= 1oxa |SIZE=350|CAPTION= <scene name='initialview01'>1oxa</scene>, resolution 2.1Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=DEB:6-DEOXYERYTHRONOLIDE+B'>DEB</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oxa OCA], [http://www.ebi.ac.uk/pdbsum/1oxa PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oxa RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Cupp-Vickery, J R.]] | [[Category: Cupp-Vickery, J R.]] | ||
[[Category: Poulos, T L.]] | [[Category: Poulos, T L.]] | ||
| - | [[Category: DEB]] | ||
| - | [[Category: HEM]] | ||
[[Category: oxidoreductase (oxygenase)]] | [[Category: oxidoreductase (oxygenase)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:51:40 2008'' |
Revision as of 19:51, 30 March 2008
| |||||||
| , resolution 2.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CYTOCHROME P450 (DONOR:O2 OXIDOREDUCTASE)
Overview
Cytochrome P450eryF catalyzes the 6S-hydroxylation of 6-deoxyerythronolide B, the initial reaction in a multistep pathway to convert 6-deoxyerythronolide B into the antibiotic, erythromycin. The overall structure of P450eryF is similar to that of P450cam but differs in the exact positioning of several alpha-helices. The largest difference occurs in the B' helix and results in the enlargement of the substrate-binding pocket of P450eryF. The substrate is positioned with the macrolide ring perpendicular to the haem plane and contacts seven hydrophobic residues and three solvent molecules. The substrate participates in a network of hydrogen bonds that may provide a proton shuttle pathway in the oxygen cleavage reaction.
About this Structure
1OXA is a Single protein structure of sequence from Saccharopolyspora erythraea. Full crystallographic information is available from OCA.
Reference
Structure of cytochrome P450eryF involved in erythromycin biosynthesis., Cupp-Vickery JR, Poulos TL, Nat Struct Biol. 1995 Feb;2(2):144-53. PMID:7749919
Page seeded by OCA on Sun Mar 30 22:51:40 2008
