3HAD
BIOCHEMICAL CHARACTERIZATION AND STRUCTURE DETERMINATION OF HUMAN HEART SHORT CHAIN L-3-HYDROXYACYL COA DEHYDROGENASE PROVIDE INSIGHT INTO CATALYTIC MECHANISM
Summary for 3HAD
Entry DOI | 10.2210/pdb3had/pdb |
Descriptor | PROTEIN (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 | 68742.05 |
Authors | Barycki, J.J.,Bratt, J.M.,Banaszak, L.J. (deposition date: 1998-12-03, release date: 2000-01-12, Last modification date: 2024-05-22) |
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 Cited by PubMed: 10231530DOI: 10.1021/bi9829027 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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