2UWH

Cytochrome P450 BM3 mutant in complex with palmitic acid

Summary for 2UWH

• Entry DOI: 10.2210/pdb2uwh/pdb
• Related: 1BU7 1BVY 1FAG 1FAH 1JME 1JPZ 1P0V 1P0W 1P0X 1SMI 1SMJ 1YQO 1YQP 2BMH 2HPD 2J1M 2J4S 2J4V 2J54
• Descriptor: BIFUNCTIONAL P-450\: NADPH-P450 REDUCTASE, PROTOPORPHYRIN IX CONTAINING FE, PALMITIC ACID, ... (4 entities in total)
• Functional Keywords: fatty-acid binding, multifunctional enzyme, metal-binding, oxidoreductase, electron transport, transport, hydroxylase, flavoprotein, monooxygenase, fmn, fad, nadp, iron, heme, redox, membrane, cytochrome p450 bm3 mutant
• Biological source: BACILLUS MEGATERIUM
• Cellular location: Cytoplasm (By similarity): P14779
• Total number of polymer chains: 6
• Total formula weight: 320074.39

Authors

Huang, W.-C.,Joyce, M.G.,Westlake, A.C.G.,Roberts, G.C.K.,Moody, P.C.E. (deposition date: 2007-03-21, release date: 2007-08-28, Last modification date: 2023-12-13)

• Primary citation: Huang, W.-C.,Westlake, A.C.G.,Marechal, J.-D.,Joyce, M.G.,Moody, P.C.E.,Roberts, G.C.K.; Filling a Hole in Cytochrome P450 Bm3 Improves Substrate Binding and Catalytic Efficiency.; J.Mol.Biol., 373:633-, 2007; PubMed: 17868686; DOI: 10.1016/J.JMB.2007.08.015

Experimental method

X-RAY DIFFRACTION (2.8 Å)