1e5t Summary



The structure was published by Fulop, V., Szeltner, Z., and Polgar, L., in 2000 in a paper entitled "Catalysis of Serine Oligopeptidases is Controlled by a Gating Filter Mechanism" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.7 Å and deposited in 2000.

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

The PDB entry contains the structure of PROLYL ENDOPEPTIDASE. This molecule has the UniProt identifier P23687 (PPCE_PIG)search. The sample contained 710 residues which is 100% of the natural sequence. Out of 710 residues 710 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 PROLYL ENDOPEPTIDASE P23687 (1-710) (PPCE_PIG)search Sus scrofasearch 100% 710 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P23687 (1 - 710) PROLYL ENDOPEPTIDASE Sus scrofa

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P23687) Prolyl oligopeptidase, N-terminal domainsearch, Prolyl oligopeptidase, C-terminal domainsearch Rossmann foldsearch, Prolyl oligopeptidase, N-terminal domainsearch PF00326: Prolyl oligopeptidase familysearch, PF02897: Prolyl oligopeptidase, N-terminal beta-propeller domainsearch

Chain ID Biological process (GO) Cellular component (GO) Molecular function (GO)
A (P23687) proteolysissearch cytoplasmsearch serine-type endopeptidase activitysearch serine-type peptidase activitysearch hydrolase activitysearch peptidase activitysearch serine-type exopeptidase activitysearch

Chain InterPro annotation
A Peptidase S9, prolyl oligopeptidase, catalytic domainsearch Peptidase S9A, prolyl oligopeptidasesearch Peptidase S9, serine active sitesearch Peptidase S9A, N-terminal domainsearch Alpha/Beta hydrolase foldsearch