1zoa
From Proteopedia
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[[Image:1zoa.png|left|200px]] | [[Image:1zoa.png|left|200px]] | ||
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===Crystal Structure Of A328V Mutant Of The Heme Domain Of P450Bm-3 With N-Palmitoylglycine=== | ===Crystal Structure Of A328V Mutant Of The Heme Domain Of P450Bm-3 With N-Palmitoylglycine=== | ||
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+ | The line below this paragraph, {{ABSTRACT_PUBMED_21875028}}, adds the Publication Abstract to the page | ||
+ | (as it appears on PubMed at http://www.pubmed.gov), where 21875028 is the PubMed ID number. | ||
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+ | {{ABSTRACT_PUBMED_21875028}} | ||
==About this Structure== | ==About this Structure== | ||
- | + | [[1zoa]] 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=1ZOA OCA]. | |
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+ | ==See Also== | ||
+ | *[[NADPH-Cytochrome P450 Reductase]] | ||
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+ | ==Reference== | ||
+ | <ref group="xtra">PMID:021875028</ref><references group="xtra"/> | ||
[[Category: Bacillus megaterium]] | [[Category: Bacillus megaterium]] | ||
[[Category: Unspecific monooxygenase]] | [[Category: Unspecific monooxygenase]] | ||
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[[Category: Cytochrome p-450]] | [[Category: Cytochrome p-450]] | ||
[[Category: Hemeprotein a328v]] | [[Category: Hemeprotein a328v]] | ||
- | + | [[Category: Oxidoreductase]] | |
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Revision as of 10:46, 14 December 2011
Contents |
Crystal Structure Of A328V Mutant Of The Heme Domain Of P450Bm-3 With N-Palmitoylglycine
Template:ABSTRACT PUBMED 21875028
About this Structure
1zoa 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
- Haines DC, Hegde A, Chen B, Zhao W, Bondlela M, Humphreys JM, Mullin DA, Tomchick DR, Machius M, Peterson JA. A single active-site mutation of P450BM-3 dramatically enhances substrate binding and rate of product formation. Biochemistry. 2011 Oct 4;50(39):8333-41. Epub 2011 Sep 6. PMID:21875028 doi:10.1021/bi201099j