Functional Information from GO Data
Chain | GOid | namespace | contents |
B | 0004252 | molecular_function | serine-type endopeptidase activity |
B | 0006508 | biological_process | proteolysis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | binding site for residue GOL A 301 |
Chain | Residue |
A | GLY196 |
A | LYS197 |
A | ILE198 |
A | LEU201 |
A | GLU202 |
B | GLY414 |
B | TRP416 |
B | GOL507 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue GOL A 302 |
Chain | Residue |
A | CYS174 |
A | SER179 |
A | LEU180 |
A | HOH403 |
A | HOH410 |
A | HOH411 |
B | HOH809 |
A | ARG173 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue CA B 501 |
Chain | Residue |
B | GLU270 |
B | ASP272 |
B | GLU275 |
B | GLU280 |
B | HOH641 |
B | HOH802 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue CL B 502 |
Chain | Residue |
B | ARG262 |
B | VAL459 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue SO4 B 503 |
Chain | Residue |
B | MET366 |
B | THR367 |
B | ARG439 |
B | HOH615 |
B | HOH622 |
B | HOH718 |
site_id | AC6 |
Number of Residues | 8 |
Details | binding site for residue SO4 B 504 |
Chain | Residue |
B | HIS253 |
B | LYS401 |
B | GLY402 |
B | SER404 |
B | 7LR508 |
B | HOH612 |
B | HOH719 |
B | HOH752 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue SO4 B 505 |
Chain | Residue |
A | HOH403 |
B | SER453 |
B | GLU454 |
B | HOH701 |
B | HOH779 |
B | HOH809 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue GOL B 506 |
Chain | Residue |
B | SER374 |
B | PRO381 |
B | HIS433 |
B | PHE434 |
B | HOH662 |
site_id | AC9 |
Number of Residues | 9 |
Details | binding site for residue GOL B 507 |
Chain | Residue |
A | ILE198 |
A | GOL301 |
B | CYS219 |
B | GLU223 |
B | LEU340 |
B | TRP416 |
B | HOH602 |
B | HOH649 |
B | HOH789 |
site_id | AD1 |
Number of Residues | 17 |
Details | binding site for residue 7LR B 508 |
Chain | Residue |
B | HIS253 |
B | ASP256 |
B | GLY297 |
B | ASP302 |
B | ASP398 |
B | SER399 |
B | CYS400 |
B | SER404 |
B | VAL422 |
B | SER423 |
B | TRP424 |
B | GLY425 |
B | GLY427 |
B | CYS428 |
B | SO4504 |
B | HOH768 |
B | HOH780 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue TFA B 509 |
Chain | Residue |
B | ASN300 |
B | HIS301 |
B | THR384 |
B | TYR386 |
B | HOH724 |
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 |
B | VAL249-CYS254 | |
site_id | PS00135 |
Number of Residues | 12 |
Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DSckGDSGGPHA |
Chain | Residue | Details |
B | ASP398-ALA409 | |
site_id | PS01186 |
Number of Residues | 16 |
Details | EGF_2 EGF-like domain signature 2. CrCheGYslladgvsC |
Chain | Residue | Details |
A | CYS172-CYS187 | |
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 |
B | HIS253 | |
B | ASP302 | |
B | SER404 | |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
B | ASP398 | |
Chain | Residue | Details |
B | ASN382 | |