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 | 4 |
| Details | BINDING SITE FOR RESIDUE SIN A 724 |
| Chain | Residue |
| A | PHE173 |
| A | ILE591 |
| A | TRP595 |
| A | GLY725 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GLY A 725 |
| Chain | Residue |
| A | ARG643 |
| A | SIN724 |
| A | PRO726 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PRO A 726 |
| Chain | Residue |
| A | SER554 |
| A | ASN555 |
| A | TRP595 |
| A | HIS680 |
| A | GLY725 |
| A | TYR473 |
| A | PHE476 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 792 |
| Chain | Residue |
| A | ALA226 |
| A | GLU227 |
| A | PHE228 |
| A | TRP262 |
| A | LYS281 |
| A | HOH2721 |
| A | HOH2722 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 793 |
| Chain | Residue |
| A | PRO568 |
| A | PHE571 |
| A | ILE628 |
| A | GLN629 |
| A | PRO631 |
| A | ASN668 |
| A | HOH2626 |
| A | HOH2723 |
| A | HOH2724 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 794 |
| Chain | Residue |
| A | GLU239 |
| A | ASP291 |
| A | TYR292 |
| A | HOH2426 |
| A | HOH2725 |
| A | HOH2726 |
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
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU10084","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1900195","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Charge relay system"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU10084","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"2064618","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"UniProtKB","id":"P48147","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P48147","evidenceCode":"ECO:0000250"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1qfm |
| Chain | Residue | Details |
| A | ALA641 | |
| 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 | ALA641 | electrostatic stabiliser, modifies pKa |
| A | HIS680 | proton shuttle (general acid/base) |
