1ZO4

Crystal Structure Of A328S Mutant Of The Heme Domain Of P450BM-3

Summary for 1ZO4

• Entry DOI: 10.2210/pdb1zo4/pdb
• Related: 1BU7 1JPZ 1ZO9 1ZOA 2HPD
• Descriptor: Bifunctional P-450:NADPH-P450 reductase, PROTOPORPHYRIN IX CONTAINING FE, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (5 entities in total)
• Functional Keywords: cytochrome p-450, hemeprotein a328s, oxidoreductase
• Biological source: Bacillus megaterium
• Cellular location: Cytoplasm (By similarity): P14779
• Total number of polymer chains: 2
• Total formula weight: 111294.17

Authors

Hegda, A.,Chen, B.,Haines, D.C.,Bondlela, M.,Mullin, D.,Graham, S.E.,Tomchick, D.R.,Machius, M.,Peterson, J.A. (deposition date: 2005-05-12, release date: 2006-08-01, Last modification date: 2023-08-23)

• Primary citation: Haines, D.C.,Hegde, A.,Chen, B.,Zhao, W.,Bondlela, M.,Humphreys, J.M.,Mullin, D.A.,Tomchick, D.R.,Machius, M.,Peterson, J.A.; A single active-site mutation of P450BM-3 dramatically enhances substrate binding and rate of product formation.; Biochemistry, 50:8333-8341, 2011; PubMed: 21875028; DOI: 10.1021/bi201099j

Experimental method

X-RAY DIFFRACTION (1.46 Å)