4BD9
Structure of the complex between SmCI and human carboxypeptidase A4
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004181 | molecular_function | metallocarboxypeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008270 | molecular_function | zinc ion binding |
| B | 0004857 | molecular_function | enzyme inhibitor activity |
| B | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0010466 | biological_process | negative regulation of peptidase activity |
| B | 0030414 | molecular_function | peptidase inhibitor activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 500 |
| Chain | Residue |
| A | HIS69 |
| A | GLU72 |
| A | HIS196 |
| A | HOH2032 |
| B | ILE1 |
Functional Information from PROSITE/UniProt
| site_id | PS00132 |
| Number of Residues | 23 |
| Details | CARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PaVwLnaGiHSrEwISQataiwT |
| Chain | Residue | Details |
| A | PRO60-THR82 |
| site_id | PS00133 |
| Number of Residues | 11 |
| Details | CARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HSYSQLLmYPY |
| Chain | Residue | Details |
| A | HIS196-TYR206 |
| site_id | PS00280 |
| Number of Residues | 19 |
| Details | BPTI_KUNITZ_1 Pancreatic trypsin inhibitor (Kunitz) family signature. FvyGGCqgnanrFetkddC |
| Chain | Residue | Details |
| B | PHE32-CYS50 | |
| B | PHE84-CYS102 | |
| B | PHE143-CYS161 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 294 |
| Details | Domain: {"description":"Peptidase M14","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23746805","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4BD9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17506531","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PCU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15738388","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16091843","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17506531","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22294694","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23746805","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2BO9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BOA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PCU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4A94","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BD9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17506531","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23746805","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PCU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BD9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15738388","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16091843","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17506531","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2BO9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BOA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PCU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 50 |
| Details | Domain: {"description":"BPTI/Kunitz inhibitor 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00031","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 50 |
| Details | Domain: {"description":"BPTI/Kunitz inhibitor 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00031","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 50 |
| Details | Domain: {"description":"BPTI/Kunitz inhibitor 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00031","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Region: {"description":"Inserts into the active site groove of a carboxypeptidase and inhibits activity by emulating a C-terminal substrate","evidences":[{"source":"PubMed","id":"23746805","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2006","submissionDatabase":"UniProtKB","title":"A novel bifunctional inhibitor of metallo carboxypeptidase and serine proteinase isolated from the annelid Sabellastarte magnifica. Isolation, characterization and cDNA cloning.","authors":["Alonso del Rivero M.","Trejo S.","Rodriguez de la Vega M.","Delfin J.","Diaz J.","Gonzalez Y.","Canals F.","Chavez M.A.","Aviles F.X."]}}]} |
| Chain | Residue | Details |
