2ij2
From Proteopedia
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[[Image:2ij2.png|left|200px]] | [[Image:2ij2.png|left|200px]] | ||
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{{STRUCTURE_2ij2| PDB=2ij2 | SCENE= }} | {{STRUCTURE_2ij2| PDB=2ij2 | SCENE= }} | ||
===Atomic structure of the heme domain of flavocytochrome P450-BM3=== | ===Atomic structure of the heme domain of flavocytochrome P450-BM3=== | ||
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{{ABSTRACT_PUBMED_17077084}} | {{ABSTRACT_PUBMED_17077084}} | ||
==About this Structure== | ==About this Structure== | ||
| - | [[2ij2]] is a 2 chain structure of [[Cytochrome P450]] with sequence from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IJ2 OCA]. | + | [[2ij2]] is a 2 chain structure of [[Cytochrome P450]], [[Flavocytochrome]] and [[NADPH-Cytochrome P450 Reductase]] with sequence from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IJ2 OCA]. |
==See Also== | ==See Also== | ||
| - | *[[Cytochrome P450]] | + | *[[Cytochrome P450|Cytochrome P450]] |
| + | *[[Flavocytochrome|Flavocytochrome]] | ||
| + | *[[NADPH-Cytochrome P450 Reductase|NADPH-Cytochrome P450 Reductase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:017077084</ref><references group="xtra"/> |
[[Category: Bacillus megaterium]] | [[Category: Bacillus megaterium]] | ||
[[Category: Unspecific monooxygenase]] | [[Category: Unspecific monooxygenase]] | ||
Revision as of 01:21, 27 July 2012
Contents |
Atomic structure of the heme domain of flavocytochrome P450-BM3
Template:ABSTRACT PUBMED 17077084
About this Structure
2ij2 is a 2 chain structure of Cytochrome P450, Flavocytochrome and NADPH-Cytochrome P450 Reductase with sequence from Bacillus megaterium. Full crystallographic information is available from OCA.
See Also
Reference
- Girvan HM, Seward HE, Toogood HS, Cheesman MR, Leys D, Munro AW. Structural and spectroscopic characterization of P450 BM3 mutants with unprecedented P450 heme iron ligand sets. New heme ligation states influence conformational equilibria in P450 BM3. J Biol Chem. 2007 Jan 5;282(1):564-72. Epub 2006 Oct 31. PMID:17077084 doi:10.1074/jbc.M607949200
