1EZS
CRYSTAL STRUCTURE OF ECOTIN MUTANT M84R, W67A, G68A, Y69A, D70A BOUND TO RAT ANIONIC TRYPSIN II
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0006952 | biological_process | defense response |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0030414 | molecular_function | peptidase inhibitor activity |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0006952 | biological_process | defense response |
| B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| B | 0030414 | molecular_function | peptidase inhibitor activity |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0042803 | molecular_function | protein homodimerization activity |
| C | 0004252 | molecular_function | serine-type endopeptidase activity |
| C | 0005509 | molecular_function | calcium ion binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005576 | cellular_component | extracellular region |
| C | 0005615 | cellular_component | extracellular space |
| C | 0006508 | biological_process | proteolysis |
| C | 0007584 | biological_process | response to nutrient |
| C | 0007586 | biological_process | digestion |
| C | 0008233 | molecular_function | peptidase activity |
| C | 0008236 | molecular_function | serine-type peptidase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0030574 | biological_process | collagen catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004252 | molecular_function | serine-type endopeptidase activity |
| D | 0005509 | molecular_function | calcium ion binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0005576 | cellular_component | extracellular region |
| D | 0005615 | cellular_component | extracellular space |
| D | 0006508 | biological_process | proteolysis |
| D | 0007584 | biological_process | response to nutrient |
| D | 0007586 | biological_process | digestion |
| D | 0008233 | molecular_function | peptidase activity |
| D | 0008236 | molecular_function | serine-type peptidase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0030574 | biological_process | collagen catabolic process |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA D 950 |
| Chain | Residue |
| D | GLU770 |
| D | ASN772 |
| D | VAL775 |
| D | GLU777 |
| D | GLU780 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA C 650 |
| Chain | Residue |
| C | GLU480 |
| C | GLU470 |
| C | ASN472 |
| C | VAL475 |
| C | GLU477 |
Functional Information from PROSITE/UniProt
| site_id | PS00134 |
| Number of Residues | 6 |
| Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC |
| Chain | Residue | Details |
| C | VAL453-CYS458 |
| site_id | PS00135 |
| Number of Residues | 12 |
| Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPVV |
| Chain | Residue | Details |
| C | ASP589-VAL600 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Site: {"description":"Reactive bond"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 440 |
| Details | Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Charge relay system"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Site: {"description":"Required for specificity","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| C | SER595 | |
| C | HIS457 | |
| C | ASN502 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| D | HIS757 | |
| D | ASN802 | |
| D | SER895 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| C | SER595 | |
| C | GLY593 | |
| C | HIS457 | |
| C | ASN502 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| D | GLY893 | |
| D | HIS757 | |
| D | ASN802 | |
| D | SER895 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| C | SER595 | |
| C | HIS457 | |
| C | GLY596 | |
| C | ASN502 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| D | HIS757 | |
| D | ASN802 | |
| D | GLY896 | |
| D | SER895 |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| C | SER595 | |
| C | GLY593 | |
| C | ASP495 | |
| C | HIS457 |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| D | GLY893 | |
| D | HIS757 | |
| D | ASP795 | |
| D | SER895 |
