Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004252 | molecular_function | serine-type endopeptidase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006508 | biological_process | proteolysis |
A | 0008233 | molecular_function | peptidase activity |
A | 0008236 | molecular_function | serine-type peptidase activity |
A | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 790 |
Chain | Residue |
A | ILE118 |
A | SER120 |
A | ASP121 |
A | ASP446 |
A | ASN522 |
A | ASN525 |
A | HOH2253 |
A | HOH2856 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 791 |
Chain | Residue |
A | GLU227 |
A | PHE228 |
A | ILE276 |
A | LYS281 |
A | HOH2857 |
A | HOH2858 |
A | ALA226 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 792 |
Chain | Residue |
A | TRP150 |
A | VAL151 |
A | THR152 |
A | GLU169 |
A | ARG170 |
A | VAL171 |
A | SER197 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 793 |
Chain | Residue |
A | PRO568 |
A | ASP569 |
A | PHE571 |
A | GLY572 |
A | ILE628 |
A | GLN629 |
A | PRO631 |
A | ASN668 |
A | HOH2859 |
A | HOH2860 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 794 |
Chain | Residue |
A | GLU239 |
A | ASP291 |
A | TYR292 |
A | HOH2431 |
A | HOH2861 |
A | HOH2862 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 795 |
Chain | Residue |
A | TRP340 |
A | VAL341 |
A | HOH2600 |
site_id | AC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 796 |
Chain | Residue |
A | PRO7 |
A | ASP8 |
A | VAL9 |
A | TRP30 |
A | GLN38 |
A | ALA41 |
A | PHE42 |
A | ALA45 |
A | HOH2863 |
A | HOH2864 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 797 |
Chain | Residue |
A | PHE173 |
A | MET235 |
A | SER250 |
A | ARG252 |
A | HOH2315 |
A | HOH2348 |
A | HOH2865 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 798 |
Chain | Residue |
A | TYR473 |
A | SER554 |
A | ASN555 |
A | TRP595 |
A | HIS680 |
A | HOH2795 |
Functional Information from PROSITE/UniProt
site_id | PS00708 |
Number of Residues | 31 |
Details | PRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DfqcAaeyLikegytspkrltinGgSnGGLL |
Chain | Residue | Details |
A | ASP529-LEU559 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | SER554 | |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Charge relay system |
Chain | Residue | Details |
A | ASP641 | |
Chain | Residue | Details |
A | HIS680 | |
Chain | Residue | Details |
A | LYS157 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1pfq |
Chain | Residue | Details |
A | ASP641 | |
A | SER554 | |
A | HIS680 | |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 901 |
Chain | Residue | Details |
A | TYR473 | electrostatic stabiliser |
A | SER554 | covalent catalysis, proton shuttle (general acid/base) |
A | ASP641 | electrostatic stabiliser, modifies pKa |
A | HIS680 | proton shuttle (general acid/base) |