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):
This entry contains 1 unique UniProt protein: