Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0016787 | molecular_function | hydrolase activity |
| B | 0004252 | molecular_function | serine-type endopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 501 |
| Chain | Residue |
| A | ARG366 |
| A | LYS367 |
| A | PHE368 |
| A | SER369 |
| B | HOH522 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BME A 403 |
| Chain | Residue |
| A | HOH500 |
| A | ASP166 |
| A | MSE175 |
| A | HIS377 |
| A | CYS378 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PGE A 404 |
| Chain | Residue |
| A | PHE238 |
| A | HOH538 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 405 |
| Chain | Residue |
| A | TYR45 |
| A | ILE46 |
| A | SER48 |
| A | GLY49 |
| A | ARG61 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 501 |
| Chain | Residue |
| A | TYR68 |
| A | HOH510 |
| B | ARG366 |
| B | LYS367 |
| B | SER369 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME B 403 |
| Chain | Residue |
| B | HIS377 |
| B | CYS378 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PGE B 404 |
| Chain | Residue |
| B | GLU206 |
| B | PHE238 |
| B | EDO405 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 405 |
| Chain | Residue |
| B | PGE404 |
| B | HOH489 |
Functional Information from PROSITE/UniProt
| site_id | PS00708 |
| Number of Residues | 31 |
| Details | PRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DaraAisaIldwyqaptekiaiaGfSgGGYF |
| Chain | Residue | Details |
| A | ASP208-PHE238 | |
