2hdh Summary

pdbe.org/2hdh
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BIOCHEMICAL CHARACTERIZATION AND STRUCTURE DETERMINATION OF HUMAN HEART SHORT CHAIN L-3-HYDROXYACYL COA DEHYDROGENASE PROVIDE INSIGHT INTO CATALYTIC MECHANISM

The structure was published by Barycki, J.J., O'Brien, L.K., Bratt, J.M., et al., Sanishvili, R., Strauss, A.W., and Banaszak, L.J., in 1999 in a paper entitled "Biochemical characterization and crystal structure determination of human heart short chain L-3-hydroxyacyl-CoA dehydrogenase provide insights into catalytic mechanism." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 1998.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of L-3-HYDROXYACYL COA DEHYDROGENASE.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homodimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A L-3-HYDROXYACYL COA DEHYDROGENASE Q16836 (24-314) (HCDH_HUMAN)search Homo sapienssearch 93% 293 100%
B L-3-HYDROXYACYL COA DEHYDROGENASE Q16836 (24-314) (HCDH_HUMAN)search Homo sapienssearch 93% 293 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q16836 (24 - 314) L-3-HYDROXYACYL COA DEHYDROGENASE Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (Q16836) HCDH C-domain-likesearch, 6-phosphogluconate dehydrogenase-like, N-terminal domainsearch NAD(P)-binding Rossmann-like Domainsearch, N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase; domain 2search PF00725: 3-hydroxyacyl-CoA dehydrogenase, C-terminal domainsearch, PF02737: 3-hydroxyacyl-CoA dehydrogenase, NAD binding domainsearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A, B (Q16836) oxidoreductase activitysearch coenzyme bindingsearch 3-hydroxyacyl-CoA dehydrogenase activitysearch oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptorsearch oxidation-reduction processsearch fatty acid metabolic processsearch fatty acid beta-oxidationsearch response to insulinsearch small molecule metabolic processsearch negative regulation of insulin secretionsearch lipid metabolic processsearch response to activitysearch response to hormonesearch cellular lipid metabolic processsearch response to drugsearch mitochondrial matrixsearch nucleolussearch cytoplasmsearch mitochondrial inner membranesearch mitochondrionsearch nucleussearch

Chain InterPro annotation
A, B 3-hydroxyacyl-CoA dehydrogenase, C-terminalsearch 3-hydroxyacyl-CoA dehydrogenase, NAD bindingsearch 3-hydroxyacyl-CoA dehydrogenase, conserved sitesearch 6-phosphogluconate dehydrogenase, C-terminal-likesearch Dehydrogenase, multihelicalsearch NAD(P)-binding domainsearch 3-hydroxyacyl-CoA dehydrogenasesearch