2HDH

BIOCHEMICAL CHARACTERIZATION AND STRUCTURE DETERMINATION OF HUMAN HEART SHORT CHAIN L-3-HYDROXYACYL COA DEHYDROGENASE PROVIDE INSIGHT INTO CATALYTIC MECHANISM

Summary for 2HDH

• Entry DOI: 10.2210/pdb2hdh/pdb
• Descriptor: L-3-HYDROXYACYL COA DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• Functional Keywords: oxidoreductase, beta oxidation, schad, catalytic activity: l-3-hydroxyacyl-coa + nad(+) = 3-oxoacyl-coa + nadh
• Biological source: Homo sapiens (human)
• Cellular location: Mitochondrion matrix: Q16836
• Total number of polymer chains: 2
• Total formula weight: 65977.12

Authors

Barycki, J.J.,Bratt, J.M.,Banaszak, L.J. (deposition date: 1998-12-04, release date: 1999-05-12, Last modification date: 2023-12-27)

• Primary citation: Barycki, J.J.,O'Brien, L.K.,Bratt, J.M.,Zhang, R.,Sanishvili, R.,Strauss, A.W.,Banaszak, L.J.; Biochemical characterization and crystal structure determination of human heart short chain L-3-hydroxyacyl-CoA dehydrogenase provide insights into catalytic mechanism.; Biochemistry, 38:5786-5798, 1999; PubMed: 10231530; DOI: 10.1021/bi9829027

Experimental method

X-RAY DIFFRACTION (2.2 Å)