Functional Information from GO Data
Chain | GOid | namespace | contents |
E | 0004252 | molecular_function | serine-type endopeptidase activity |
E | 0006508 | biological_process | proteolysis |
E | 0008236 | molecular_function | serine-type peptidase activity |
I | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
I | 0005576 | cellular_component | extracellular region |
I | 0010466 | biological_process | negative regulation of peptidase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA E 501 |
Chain | Residue |
E | GLN2 |
E | ASP41 |
E | LEU75 |
E | ASN77 |
E | ILE79 |
E | VAL81 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA E 502 |
Chain | Residue |
E | GLY169 |
E | TYR171 |
E | VAL174 |
E | GLU195 |
E | ASP197 |
E | HOH725 |
E | HOH726 |
site_id | CAT |
Number of Residues | 3 |
Details | catalytic site |
Chain | Residue |
E | ASP32 |
E | HIS64 |
E | SER221 |
site_id | RAC |
Number of Residues | 2 |
Details | TWO RESIDUES OF inhibitor CONNECTED THROUGH A REACTIVE SITE PEPTIDE BOND (OR A SCISSILE BOND) WHICH IS POTENTIALLY CLEAVED BY THE TARGET ENZYME, SUBTILISIN. |
site_id | S13 |
Number of Residues | 3 |
Details | S1-3 SITE AND COMPRISES A THREE-RESIDUE POLYPEPTIDE SEGMENT IN SUBTILISIN CAPABLE OF FORMING AN ANTIPARALLEL BETA-SHEET WITH THE P1, P2, AND P3 RESIDUES OF the inhibitor. |
Chain | Residue |
E | SER125 |
E | LEU126 |
E | GLY127 |
site_id | S46 |
Number of Residues | 3 |
Details | S4-6 SITE AND COMPRISES A THREE-RESIDUE POLYPEPTIDE SEGMENT IN SUBTILISIN CAPABLE OF FORMING AN ANTIPARALLEL BETA-SHEET WITH THE P4, P5 AND P6 RESIDUES OF inhibitor |
Chain | Residue |
E | GLY102 |
E | GLN103 |
E | TYR104 |
Functional Information from PROSITE/UniProt
site_id | PS00136 |
Number of Residues | 12 |
Details | SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVIDSGIdssH |
Chain | Residue | Details |
E | VAL28-HIS39 | |
site_id | PS00137 |
Number of Residues | 11 |
Details | SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGtVAA |
Chain | Residue | Details |
E | HIS64-ALA74 | |
site_id | PS00138 |
Number of Residues | 11 |
Details | SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAsPhVAG |
Chain | Residue | Details |
E | GLY219-GLY229 | |
site_id | PS00999 |
Number of Residues | 19 |
Details | SSI Streptomyces subtilisin-type inhibitors signature. CaPgpsGtHPaagsACAdL |
Chain | Residue | Details |
I | CYS35-LEU53 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | SITE: Reactive bond for subtilisin |
Chain | Residue | Details |
I | MET73 | |
E | HIS64 | |
E | SER221 | |
site_id | SWS_FT_FI2 |
Number of Residues | 9 |
Details | BINDING: |
Chain | Residue | Details |
E | GLN2 | |
E | ASP41 | |
E | LEU75 | |
E | ASN77 | |
E | ILE79 | |
E | VAL81 | |
E | GLY169 | |
E | TYR171 | |
E | VAL174 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1sca |
Chain | Residue | Details |
E | SER221 | |
E | HIS64 | |
E | ASP32 | |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 723 |
Chain | Residue | Details |
E | ASP32 | electrostatic interaction, electrostatic stabiliser |
E | HIS64 | proton acceptor, proton donor |
E | ASN155 | electrostatic interaction, electrostatic stabiliser |
E | SER221 | nucleofuge, nucleophile, proton acceptor, proton donor |