4kpb
From Proteopedia
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- | + | {{STRUCTURE_4kpb| PDB=4kpb | SCENE= }} | |
+ | ===Crystal structure of cytochrome P450 BM-3 R47E mutant=== | ||
+ | {{ABSTRACT_PUBMED_23829560}} | ||
- | The | + | ==Function== |
+ | [[http://www.uniprot.org/uniprot/CPXB_BACME CPXB_BACME]] Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of medium and long-chain fatty acids at omega-1, omega-2 and omega-3 positions, with optimum chain lengths of 12-16 carbons (lauric, myristic, and palmitic acids). The reductase domain is required for electron transfer from NADP to cytochrome P450. | ||
- | + | ==About this Structure== | |
+ | [[4kpb]] is a 2 chain structure 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=4KPB OCA]. | ||
- | + | ==Reference== | |
+ | <ref group="xtra">PMID:023829560</ref><references group="xtra"/><references/> | ||
+ | [[Category: Bacillus megaterium]] | ||
+ | [[Category: Unspecific monooxygenase]] | ||
+ | [[Category: Catalano, J.]] | ||
+ | [[Category: McDermott, A E.]] | ||
+ | [[Category: Sadre-Bazzaz, K.]] | ||
+ | [[Category: Tong, L.]] | ||
+ | [[Category: Heme-dependent stereospecific oxidation of substrate]] | ||
+ | [[Category: Oxidoreductase]] |
Revision as of 12:58, 24 July 2013
Contents |
Crystal structure of cytochrome P450 BM-3 R47E mutant
Template:ABSTRACT PUBMED 23829560
Function
[CPXB_BACME] Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of medium and long-chain fatty acids at omega-1, omega-2 and omega-3 positions, with optimum chain lengths of 12-16 carbons (lauric, myristic, and palmitic acids). The reductase domain is required for electron transfer from NADP to cytochrome P450.
About this Structure
4kpb is a 2 chain structure with sequence from Bacillus megaterium. Full crystallographic information is available from OCA.
Reference
- Catalano J, Sadre-Bazzaz K, Amodeo GA, Tong L, McDermott AE. Structural Evidence: A Single Charged Residue Affects Substrate Binding in Cytochrome P450 BM-3. Biochemistry. 2013 Jul 6. PMID:23829560 doi:10.1021/bi4000645