4kf2

Structure of the P4509 BM3 A82F F87V heme domainStructure of the P4509 BM3 A82F F87V heme domain

FunctionFunction

[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 StructureAbout this Structure

4kf2 is a 2 chain structure with sequence from Bacillus megaterium. Full crystallographic information is available from OCA.

ReferenceReference

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↑ Butler CF, Peet C, Mason AE, Voice MW, Leys D, Munro AW. Key Mutations Alter the Cytochrome P450 BM3 Conformational Landscape and Remove Inherent Substrate Bias. J Biol Chem. 2013 Aug 30;288(35):25387-99. doi: 10.1074/jbc.M113.479717. Epub, 2013 Jul 3. PMID:23828198 doi:10.1074/jbc.M113.479717

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OCA

[1] Butler CF, Peet C, Mason AE, Voice MW, Leys D, Munro AW. Key Mutations Alter the Cytochrome P450 BM3 Conformational Landscape and Remove Inherent Substrate Bias. J Biol Chem. 2013 Aug 30;288(35):25387-99. doi: 10.1074/jbc.M113.479717. Epub, 2013 Jul 3. PMID:23828198 doi:10.1074/jbc.M113.479717

[xtra 1]