1K9X
Structure of Pyrococcus furiosus carboxypeptidase Apo-Yb
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004180 | molecular_function | carboxypeptidase activity |
| A | 0004181 | molecular_function | metallocarboxypeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046914 | molecular_function | transition metal ion binding |
| A | 0050897 | molecular_function | cobalt ion binding |
| B | 0004180 | molecular_function | carboxypeptidase activity |
| B | 0004181 | molecular_function | metallocarboxypeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0008237 | molecular_function | metallopeptidase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0046914 | molecular_function | transition metal ion binding |
| B | 0050897 | molecular_function | cobalt ion binding |
| C | 0004180 | molecular_function | carboxypeptidase activity |
| C | 0004181 | molecular_function | metallocarboxypeptidase activity |
| C | 0006508 | biological_process | proteolysis |
| C | 0008233 | molecular_function | peptidase activity |
| C | 0008237 | molecular_function | metallopeptidase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0046914 | molecular_function | transition metal ion binding |
| C | 0050897 | molecular_function | cobalt ion binding |
| D | 0004180 | molecular_function | carboxypeptidase activity |
| D | 0004181 | molecular_function | metallocarboxypeptidase activity |
| D | 0006508 | biological_process | proteolysis |
| D | 0008233 | molecular_function | peptidase activity |
| D | 0008237 | molecular_function | metallopeptidase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0046914 | molecular_function | transition metal ion binding |
| D | 0050897 | molecular_function | cobalt ion binding |
Functional Information from PROSITE/UniProt
| site_id | PS00142 |
| Number of Residues | 10 |
| Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. STVHEFGHAL |
| Chain | Residue | Details |
| A | SER266-LEU275 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1972 |
| Details | Domain: {"description":"Peptidase M32","evidences":[{"source":"PROSITE-ProRule","id":"PRU01378","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Motif: {"description":"HPF","evidences":[{"source":"PROSITE-ProRule","id":"PRU01378","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Motif: {"description":"DXRXT","evidences":[{"source":"PROSITE-ProRule","id":"PRU01378","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | Motif: {"description":"HEXXH","evidences":[{"source":"PROSITE-ProRule","id":"PRU01378","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | Motif: {"description":"HES/GQ","evidences":[{"source":"PROSITE-ProRule","id":"PRU01378","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 20 |
| Details | Motif: {"description":"I/NRXXA/SD","evidences":[{"source":"PROSITE-ProRule","id":"PRU01378","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 28 |
| Details | Motif: {"description":"GXXQDXHW","evidences":[{"source":"PROSITE-ProRule","id":"PRU01378","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01378","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11839307","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1i1i |
| Chain | Residue | Details |
| A | TYR423 | |
| A | GLU299 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1i1i |
| Chain | Residue | Details |
| B | TYR423 | |
| B | GLU299 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1i1i |
| Chain | Residue | Details |
| C | TYR423 | |
| C | GLU299 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1i1i |
| Chain | Residue | Details |
| D | TYR423 | |
| D | GLU299 |
