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 | 0005515 | molecular_function | protein binding |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006954 | biological_process | inflammatory response |
| B | 0008191 | molecular_function | metalloendopeptidase inhibitor activity |
| B | 0008201 | molecular_function | heparin binding |
| B | 0030414 | molecular_function | peptidase inhibitor activity |
| C | 0004181 | molecular_function | metallocarboxypeptidase activity |
| C | 0006508 | biological_process | proteolysis |
| C | 0008270 | molecular_function | zinc ion binding |
| D | 0004857 | molecular_function | enzyme inhibitor activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005615 | cellular_component | extracellular space |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006954 | biological_process | inflammatory response |
| D | 0008191 | molecular_function | metalloendopeptidase inhibitor activity |
| D | 0008201 | molecular_function | heparin binding |
| D | 0030414 | molecular_function | peptidase inhibitor activity |
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 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 588 |
| 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 | 2 |
| 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 | 6 |
| 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 | 6 |
| 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 | 2 |
| 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 | 2 |
| 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 | 192 |
| Details | Domain: {"description":"Cystatin LXN-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01377","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 38 |
| Details | Region: {"description":"Alpha-helical linker","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cbx |
| Chain | Residue | Details |
| A | ARG127 | |
| A | GLU270 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cbx |
| Chain | Residue | Details |
| C | ARG127 | |
| C | GLU270 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cbx |
| Chain | Residue | Details |
| A | ARG71 | |
| A | GLU270 | |
| A | ARG127 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cbx |
| Chain | Residue | Details |
| C | ARG71 | |
| C | GLU270 | |
| C | ARG127 |
