1afw Summary

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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):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A 3-KETOACETYL-COA THIOLASE P27796 (25-417) (THIK_YEAST)search Saccharomyces cerevisiae S288csearch 94% 393 100%
B 3-KETOACETYL-COA THIOLASE P27796 (25-417) (THIK_YEAST)search Saccharomyces cerevisiae S288csearch 94% 393 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P27796 (25 - 417) 3-KETOACETYL-COA THIOLASE Saccharomyces cerevisiae

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P27796) Thiolase-relatedsearch Peroxisomal Thiolase; Chain A, domain 1search PF00108: Thiolase, N-terminal domainsearch, PF02803: Thiolase, C-terminal domainsearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A, B (P27796) metabolic processsearch fatty acid metabolic processsearch lipid metabolic processsearch fatty acid beta-oxidationsearch transferase activity, transferring acyl groups other than amino-acyl groupssearch catalytic activitysearch protein bindingsearch acetyl-CoA C-acyltransferase activitysearch transferase activity, transferring acyl groupssearch mRNA bindingsearch transferase activitysearch mitochondrial intermembrane spacesearch peroxisomesearch peroxisomal matrixsearch

Chain InterPro annotation
A, B Thiolasesearch Thiolase-like, subgroupsearch Thiolase-likesearch Thiolase, active sitesearch Thiolase, conserved sitesearch Thiolase, acyl-enzyme intermediate active sitesearch Thiolase, N-terminalsearch Thiolase, C-terminalsearch