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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 DOI10.2210/pdb3had/pdb
DescriptorPROTEIN (L-3-HYDROXYACYL COA DEHYDROGENASE), NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
Functional Keywordsoxidoreductase, beta oxidation, schad, catalytic activity: l-3-hydroxyacyl-coa + nad(+) = 3-oxoacyl-coa + nadh
Biological sourceHomo sapiens (human)
Cellular locationMitochondrion matrix: Q16836
Total number of polymer chains2
Total formula weight68742.05
Authors
Barycki, J.J.,Bratt, J.M.,Banaszak, L.J. (deposition date: 1998-12-03, release date: 2000-01-12, Last modification date: 2022-12-21)
Primary citationBarycki, 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: 10231530
DOI: 10.1021/bi9829027
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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