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 | 0010466 | biological_process | negative regulation of peptidase activity |
A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
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 | 0010466 | biological_process | negative regulation of peptidase activity |
B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
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 | 0008236 | molecular_function | serine-type peptidase 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 | 0008236 | molecular_function | serine-type peptidase 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 | 6 |
Details | ACT_SITE: Charge relay system |
Chain | Residue | Details |
C | HIS457 | |
C | ASN502 | |
C | SER595 | |
D | HIS757 | |
D | ASN802 | |
D | SER895 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: |
Chain | Residue | Details |
C | GLU470 | |
C | ASN472 | |
C | VAL475 | |
C | GLU480 | |
D | GLU770 | |
D | ASN772 | |
D | VAL775 | |
D | GLU780 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Required for specificity => ECO:0000250 |
Chain | Residue | Details |
C | ASP589 | |
D | ASP889 |
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 |