Functional Information from GO Data
Chain | GOid | namespace | contents |
C | 0004252 | molecular_function | serine-type endopeptidase activity |
C | 0006508 | biological_process | proteolysis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 301 |
Chain | Residue |
A | SER163 |
A | ASP164 |
A | HOH405 |
C | ARG331 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue GOL A 302 |
Chain | Residue |
C | HIS411 |
C | GLY414 |
C | THR415 |
C | TRP416 |
A | GLY196 |
A | LYS197 |
A | ILE198 |
A | LEU201 |
A | GLU202 |
site_id | AC3 |
Number of Residues | 10 |
Details | binding site for residue GOL A 303 |
Chain | Residue |
A | ARG173 |
A | CYS174 |
A | SER179 |
A | LEU180 |
A | HOH401 |
A | HOH403 |
A | HOH406 |
A | HOH407 |
A | HOH433 |
A | HOH449 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue CA C 501 |
Chain | Residue |
C | GLU270 |
C | ASP272 |
C | GLU275 |
C | GLU280 |
C | HOH648 |
C | HOH791 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue CL C 503 |
Chain | Residue |
C | ARG262 |
C | GLY458 |
C | VAL459 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue CL C 504 |
Chain | Residue |
C | ARG284 |
C | GLN310 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue SO4 C 505 |
Chain | Residue |
C | MET366 |
C | THR367 |
C | ARG439 |
C | HOH634 |
C | HOH694 |
C | HOH786 |
site_id | AC8 |
Number of Residues | 8 |
Details | binding site for residue GOL C 506 |
Chain | Residue |
C | PHE255 |
C | TRP261 |
C | ILE290 |
C | PRO296 |
C | HOH620 |
C | HOH651 |
C | HOH654 |
C | HOH737 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue GOL C 507 |
Chain | Residue |
A | TYR193 |
C | ASP279 |
C | THR315 |
C | ASP316 |
C | HIS317 |
C | HOH655 |
C | HOH751 |
site_id | AD1 |
Number of Residues | 9 |
Details | binding site for residue GOL C 508 |
Chain | Residue |
A | LEU180 |
A | ALA182 |
C | GLN236 |
C | THR353 |
C | LEU355 |
C | HOH615 |
C | HOH696 |
C | HOH705 |
C | HOH754 |
site_id | AD2 |
Number of Residues | 14 |
Details | binding site for residue 7ZM C 509 |
Chain | Residue |
C | HIS253 |
C | CYS254 |
C | ASP398 |
C | SER399 |
C | CYS400 |
C | LYS401 |
C | SER404 |
C | VAL422 |
C | SER423 |
C | TRP424 |
C | GLY425 |
C | GLY427 |
C | HOH617 |
C | HOH672 |
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 | VAL249-CYS254 | |
site_id | PS00135 |
Number of Residues | 12 |
Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DSckGDSGGPHA |
Chain | Residue | Details |
C | 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 |
C | HIS253 | |
C | ASP302 | |
C | SER404 | |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
C | ASP398 | |
Chain | Residue | Details |
C | ASN382 | |