1bu7: Difference between revisions
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|PDB= 1bu7 |SIZE=350|CAPTION= <scene name='initialview01'>1bu7</scene>, resolution 1.65Å | |PDB= 1bu7 |SIZE=350|CAPTION= <scene name='initialview01'>1bu7</scene>, resolution 1.65Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bu7 OCA], [http://www.ebi.ac.uk/pdbsum/1bu7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bu7 RCSB]</span> | |||
}} | }} | ||
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[[Category: Li, H.]] | [[Category: Li, H.]] | ||
[[Category: Poulos, T L.]] | [[Category: Poulos, T L.]] | ||
[[Category: fatty acid monooxygenase]] | [[Category: fatty acid monooxygenase]] | ||
[[Category: hemoprotein]] | [[Category: hemoprotein]] | ||
[[Category: p450]] | [[Category: p450]] | ||
''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 19:08:19 2008'' | ||
Revision as of 16:08, 30 March 2008
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| 1bu7, resolution 1.65Å | |||||||||||||
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| Ligands: | EDO, HEM | ||||||||||||
| Activity: | Unspecific monooxygenase, with EC number 1.14.14.1 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CRYOGENIC STRUCTURE OF CYTOCHROME P450BM-3 HEME DOMAIN
Overview
The crystal structure of the complex between the heme- and FMN-binding domains of bacterial cytochrome P450BM-3, a prototype for the complex between eukaryotic microsomal P450s and P450 reductase, has been determined at 2.03 A resolution. The flavodoxin-like flavin domain is positioned at the proximal face of the heme domain with the FMN 4.0 and 18.4 A from the peptide that precedes the heme-binding loop and the heme iron, respectively. The heme-binding peptide represents the most efficient and coupled through-bond electron pathway to the heme iron. Substantial differences between the FMN-binding domains of P450BM-3 and microsomal P450 reductase, observed around the flavin-binding sites, are responsible for different redox properties of the FMN, which, in turn, control electron flow to the P450.
About this Structure
1BU7 is a Single protein structure of sequence from Bacillus megaterium. Full crystallographic information is available from OCA.
Reference
Structure of a cytochrome P450-redox partner electron-transfer complex., Sevrioukova IF, Li H, Zhang H, Peterson JA, Poulos TL, Proc Natl Acad Sci U S A. 1999 Mar 2;96(5):1863-8. PMID:10051560
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