1WPX
Crystal structure of carboxypeptidase Y inhibitor complexed with the cognate proteinase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004185 | molecular_function | serine-type carboxypeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| B | 0000328 | cellular_component | fungal-type vacuole lumen |
| B | 0000329 | cellular_component | fungal-type vacuole membrane |
| B | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005543 | molecular_function | phospholipid binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0030162 | biological_process | regulation of proteolysis |
| B | 0030414 | molecular_function | peptidase inhibitor activity |
| B | 0046578 | biological_process | regulation of Ras protein signal transduction |
Functional Information from PROSITE/UniProt
| site_id | PS00131 |
| Number of Residues | 8 |
| Details | CARBOXYPEPT_SER_SER Serine carboxypeptidases, serine active site. IaGESYAG |
| Chain | Residue | Details |
| A | ILE142-GLY149 |
| site_id | PS00560 |
| Number of Residues | 18 |
| Details | CARBOXYPEPT_SER_HIS Serine carboxypeptidases, histidine active site. FtyLrVfNGGHmVPfdvP |
| Chain | Residue | Details |
| A | PHE387-PRO404 |
| site_id | PS01220 |
| Number of Residues | 23 |
| Details | PBP Phosphatidylethanolamine-binding protein family signature. FtLVmTDPDaPSktdhkwsefcH |
| Chain | Residue | Details |
| B | PHE589-HIS611 |
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 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"12473200","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bcr |
| Chain | Residue | Details |
| A | GLY53 | |
| A | TYR147 | |
| A | SER146 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bcr |
| Chain | Residue | Details |
| A | ASP338 | |
| A | HIS397 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bcr |
| Chain | Residue | Details |
| A | ASP338 | |
| A | HIS397 | |
| A | SER146 |
