4S2R
Crystal structure of X-prolyl aminopeptidase from Caenorhabditis elegans: a cytosolic enzyme with a di-nuclear active site
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| P | 0004177 | molecular_function | aminopeptidase activity |
| P | 0005737 | cellular_component | cytoplasm |
| P | 0006508 | biological_process | proteolysis |
| P | 0008233 | molecular_function | peptidase activity |
| P | 0008270 | molecular_function | zinc ion binding |
| P | 0016787 | molecular_function | hydrolase activity |
| P | 0042803 | molecular_function | protein homodimerization activity |
| P | 0046872 | molecular_function | metal ion binding |
| P | 0051603 | biological_process | proteolysis involved in protein catabolic process |
| P | 0070006 | molecular_function | metalloaminopeptidase activity |
| Q | 0004177 | molecular_function | aminopeptidase activity |
| Q | 0005737 | cellular_component | cytoplasm |
| Q | 0006508 | biological_process | proteolysis |
| Q | 0008233 | molecular_function | peptidase activity |
| Q | 0008270 | molecular_function | zinc ion binding |
| Q | 0016787 | molecular_function | hydrolase activity |
| Q | 0042803 | molecular_function | protein homodimerization activity |
| Q | 0046872 | molecular_function | metal ion binding |
| Q | 0051603 | biological_process | proteolysis involved in protein catabolic process |
| Q | 0070006 | molecular_function | metalloaminopeptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN P 701 |
| Chain | Residue |
| P | ASP424 |
| P | HIS487 |
| P | GLU522 |
| P | GLU536 |
| P | ZN702 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN P 702 |
| Chain | Residue |
| P | ZN701 |
| P | ASP413 |
| P | ASP424 |
| P | THR426 |
| P | GLU536 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN Q 701 |
| Chain | Residue |
| Q | PHE378 |
| Q | ASP413 |
| Q | ASP424 |
| Q | THR426 |
| Q | GLU536 |
| Q | ZN702 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN Q 702 |
| Chain | Residue |
| Q | ASP424 |
| Q | HIS487 |
| Q | GLU522 |
| Q | GLU536 |
| Q | ZN701 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25905034","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4S2T","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25905034","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4S2R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4S2T","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |






