1CPY
SITE-DIRECTED MUTAGENESIS ON (SERINE) CARBOXYPEPTIDASE Y FROM YEAST. THE SIGNIFICANCE OF THR 60 AND MET 398 IN HYDROLYSIS AND AMINOLYSIS REACTIONS
Functional Information from GO Data
Functional Information from PDB Data
| site_id | CAT |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| A | SER146 |
| A | ASP338 |
| A | HIS397 |
| A | ALA145 |
| site_id | CBS |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| A | ASN51 |
| A | GLY52 |
| A | ALA145 |
| A | HIS397 |
| site_id | S1P |
| Number of Residues | 7 |
| Details |
| Chain | Residue |
| A | PHE64 |
| A | ALA65 |
| A | TYR256 |
| A | TYR269 |
| A | LEU272 |
| A | MET398 |
| A | THR60 |
| site_id | S1S |
| Number of Residues | 6 |
| Details |
| Chain | Residue |
| A | TYR147 |
| A | LEU178 |
| A | LEU245 |
| A | TRP312 |
| A | ILE340 |
| A | CYS341 |
Functional Information from PROSITE/UniProt
| site_id | PS00560 |
| Number of Residues | 18 |
| Details | CARBOXYPEPT_SER_HIS Serine carboxypeptidases, histidine active site. FtyLrVfNGGHmVPfdvP |
| Chain | Residue | Details |
| A | PHE387-PRO404 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"7727362","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1984","firstPage":"639","lastPage":"645","volume":"49","journal":"Carlsberg Res. Commun.","title":"Identification of methionyl and cysteinyl residues in the substrate binding site of carboxypeptidase Y.","authors":["Breddam K.","Svendsen I."],"citationCrossReferences":[{"database":"DOI","id":"10.1007/BF02907496"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"7727362","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"2639680","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7727362","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"journal article","publicationDate":"1984","firstPage":"639","lastPage":"645","volume":"49","journal":"Carlsberg Res. Commun.","title":"Identification of methionyl and cysteinyl residues in the substrate binding site of carboxypeptidase Y.","authors":["Breddam K.","Svendsen I."],"citationCrossReferences":[{"database":"DOI","id":"10.1007/BF02907496"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (high mannose) asparagine","evidences":[{"source":"PubMed","id":"28189789","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (high mannose) asparagine","evidences":[{"source":"PubMed","id":"15713484","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28189789","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7727362","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1bcr |
| Chain | Residue | Details |
| A | ASP338 | |
| A | GLY53 | |
| A | TYR147 | |
| A | HIS397 | |
| A | SER146 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bcr |
| Chain | Residue | Details |
| A | ASP338 | |
| A | HIS397 | |
| A | SER146 |
