1bvy: Difference between revisions
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|PDB= 1bvy |SIZE=350|CAPTION= <scene name='initialview01'>1bvy</scene>, resolution 2.03Å | |PDB= 1bvy |SIZE=350|CAPTION= <scene name='initialview01'>1bvy</scene>, resolution 2.03Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=1bvy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bvy OCA], [http://www.ebi.ac.uk/pdbsum/1bvy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bvy RCSB]</span> | |||
}} | }} | ||
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[[Category: Sevrioukova, I F.]] | [[Category: Sevrioukova, I F.]] | ||
[[Category: Zhang, H.]] | [[Category: Zhang, H.]] | ||
[[Category: electron transfer]] | [[Category: electron transfer]] | ||
[[Category: fatty acid monooxygenase]] | [[Category: fatty acid monooxygenase]] | ||
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[[Category: hemoprotein]] | [[Category: hemoprotein]] | ||
''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 19:09:23 2008'' | ||
Revision as of 19:09, 30 March 2008
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| , resolution 2.03Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | Unspecific monooxygenase, with EC number 1.14.14.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
COMPLEX OF THE HEME AND FMN-BINDING DOMAINS OF THE CYTOCHROME P450(BM-3)
OverviewOverview
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 StructureAbout this Structure
1BVY is a Protein complex structure of sequences from Bacillus megaterium. Full crystallographic information is available from OCA.
ReferenceReference
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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