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1F0Y

L-3-HYDROXYACYL-COA DEHYDROGENASE COMPLEXED WITH ACETOACETYL-COA AND NAD+

Summary for 1F0Y
Entry DOI10.2210/pdb1f0y/pdb
Related1F12 1F14 1F17 3HAD
DescriptorL-3-HYDROXYACYL-COA DEHYDROGENASE, ACETOACETYL-COENZYME A, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (4 entities in total)
Functional Keywordsabortive ternary complex, oxidoreductase
Biological sourceHomo sapiens (human)
Cellular locationMitochondrion matrix: Q16836
Total number of polymer chains2
Total formula weight68767.49
Authors
Barycki, J.J.,O'Brien, L.K.,Strauss, A.W.,Banaszak, L.J. (deposition date: 2000-05-17, release date: 2000-09-01, Last modification date: 2024-02-07)
Primary citationBarycki, J.J.,O'Brien, L.K.,Strauss, A.W.,Banaszak, L.J.
Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase.
J.Biol.Chem., 275:27186-27196, 2000
Cited by
PubMed: 10840044
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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