1oxa
From Proteopedia
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|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> | ||
}} | }} | ||
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[[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
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| , 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
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