Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004252 | molecular_function | serine-type endopeptidase activity |
A | 0006508 | biological_process | proteolysis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SO4 A 203 |
Chain | Residue |
A | ARG25 |
A | HOH361 |
A | HOH398 |
A | ARG78 |
A | GLN190 |
A | TYR191 |
A | HOH230 |
A | HOH231 |
A | HOH232 |
A | HOH359 |
A | HOH360 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 A 204 |
Chain | Residue |
A | ALA1 |
A | ASN2 |
A | ARG183 |
A | PRO186 |
A | HOH208 |
A | HOH267 |
A | HOH324 |
A | HOH325 |
A | HOH377 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 205 |
Chain | Residue |
A | HIS36 |
A | ARG89 |
A | ARG140 |
A | GLY141 |
A | SER143 |
A | HOH341 |
A | HOH342 |
A | HOH343 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 206 |
Chain | Residue |
A | THR92 |
A | ARG105 |
A | HOH327 |
A | HOH421 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 201 |
Chain | Residue |
A | HIS36 |
A | ARG89 |
A | TYR123 |
A | GLU125 |
A | SER159 |
A | GLY160 |
A | HOH277 |
A | HOH329 |
A | HOH401 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 202 |
Chain | Residue |
A | THR106 |
A | THR107 |
A | THR107 |
A | TYR109 |
A | GLN110 |
A | CYS170 |
A | HOH239 |
A | HOH431 |
Functional Information from PROSITE/UniProt
site_id | PS00134 |
Number of Residues | 6 |
Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAGHC |
Chain | Residue | Details |
A | VAL32-CYS37 | |
site_id | PS00135 |
Number of Residues | 12 |
Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. CMgrGDSGGSWI |
Chain | Residue | Details |
A | CYS137-ILE148 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | ACT_SITE: Charge relay system => ECO:0000250 |
Chain | Residue | Details |
A | HIS36 | |
A | ASP63 | |
A | SER143 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1ssx |
Chain | Residue | Details |
A | SER143 | |
A | GLY141 | |
A | ASP63 | |
A | HIS36 | |
A | SER159 | |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1ssx |
Chain | Residue | Details |
A | SER143 | |
A | GLY141 | |
A | ASP63 | |
A | HIS36 | |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 609 |
Chain | Residue | Details |
A | HIS36 | proton acceptor, proton donor |
A | ASP63 | electrostatic stabiliser |
A | GLY141 | electrostatic stabiliser |
A | SER143 | electrostatic stabiliser |
A | SER159 | electrostatic stabiliser |