THE 1.8 ANGSTROM CRYSTAL STRUCTURE OF THE DIMERIC PEROXISOMAL THIOLASE OF SACCHAROMYCES CEREVISIAE
The structure was published by Mathieu, M., Modis, Y., Zeelen, J.P., et al., Lamzin, V.S., Kunau, W.H., and Wierenga, R.K., in 1997 in a paper entitled "The 1.8 A crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: implications for substrate binding and reaction mechanism." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 1997.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of 3-KETOACETYL-COA THIOLASE.
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: