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1yqo
From Proteopedia
(Difference between revisions)
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[[Image:1yqo.png|left|200px]] | [[Image:1yqo.png|left|200px]] | ||
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{{STRUCTURE_1yqo| PDB=1yqo | SCENE= }} | {{STRUCTURE_1yqo| PDB=1yqo | SCENE= }} | ||
===T268A mutant heme domain of flavocytochrome P450 BM3=== | ===T268A mutant heme domain of flavocytochrome P450 BM3=== | ||
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{{ABSTRACT_PUBMED_16403573}} | {{ABSTRACT_PUBMED_16403573}} | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[1yqo]] is a 2 chain structure of [[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=1YQO OCA]. | |
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| + | ==See Also== | ||
| + | *[[NADPH-Cytochrome P450 Reductase|NADPH-Cytochrome P450 Reductase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:016403573</ref><ref group="xtra">PMID:015740751</ref><references group="xtra"/> |
[[Category: Bacillus megaterium]] | [[Category: Bacillus megaterium]] | ||
[[Category: Chapman, S K.]] | [[Category: Chapman, S K.]] | ||
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[[Category: Cytochrome p450]] | [[Category: Cytochrome p450]] | ||
[[Category: Fatty acid hydroxylase]] | [[Category: Fatty acid hydroxylase]] | ||
| - | + | [[Category: Oxidoreductase]] | |
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Revision as of 16:31, 25 July 2012
Contents |
T268A mutant heme domain of flavocytochrome P450 BM3
Template:ABSTRACT PUBMED 16403573
About this Structure
1yqo is a 2 chain structure of NADPH-Cytochrome P450 Reductase with sequence from Bacillus megaterium. Full crystallographic information is available from OCA.
See Also
Reference
- Clark JP, Miles CS, Mowat CG, Walkinshaw MD, Reid GA, Daff SN, Chapman SK. The role of Thr268 and Phe393 in cytochrome P450 BM3. J Inorg Biochem. 2006 May;100(5-6):1075-90. Epub 2006 Jan 5. PMID:16403573 doi:10.1016/j.jinorgbio.2005.11.020
- DeLaBarre B, Brunger AT. Nucleotide dependent motion and mechanism of action of p97/VCP. J Mol Biol. 2005 Mar 25;347(2):437-52. PMID:15740751 doi:http://dx.doi.org/10.1016/j.jmb.2005.01.060
