1ysc Summary

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2.8 ANGSTROMS STRUCTURE OF YEAST SERINE CARBOXYPEPTIDASE

The structure was published by Endrizzi, J.A., Breddam, K., and Remington, S.J., in 1994 in a paper entitled "2.8-A structure of yeast serine carboxypeptidase" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.8 Å and deposited in 1994.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of SERINE CARBOXYPEPTIDASE. This molecule has the UniProt identifier P00729 (CBPY_YEAST)search. The sample contained 421 residues which is < 90% of the natural sequence. Out of 421 residues 410 were observed and are deposited in the PDB.

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 is most likely monomeric.

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 SERINE CARBOXYPEPTIDASE P00729 (112-532) (CBPY_YEAST)search Saccharomyces cerevisiae S288csearch < 90% 421 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00729 (112 - 532) SERINE CARBOXYPEPTIDASE Saccharomyces cerevisiae

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A Serine carboxypeptidase-likesearch Rossmann foldsearch, Helix Hairpinssearch Serine carboxypeptidasesearch

Chain ID Biological process (GO) Molecular function (GO)
A (P00729) proteolysissearch serine-type carboxypeptidase activitysearch

Chain InterPro annotation
A Peptidase S10, serine carboxypeptidasesearch Peptidase S10, serine carboxypeptidase, active sitesearch Alpha/Beta hydrolase foldsearch