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 | 0008236 | molecular_function | serine-type peptidase activity |
| A | 0008242 | molecular_function | omega peptidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| B | 0004252 | molecular_function | serine-type endopeptidase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006508 | biological_process | proteolysis |
| B | 0008236 | molecular_function | serine-type peptidase activity |
| B | 0008242 | molecular_function | omega peptidase activity |
| B | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GLY A 1001 |
| Chain | Residue |
| A | PHE485 |
| A | ARG526 |
| A | PHE1002 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PHE A 1002 |
| Chain | Residue |
| A | ARG526 |
| A | THR527 |
| A | HIS556 |
| A | GLY1001 |
| A | GLY368 |
| A | GLY369 |
| A | SER445 |
| A | TYR446 |
| A | MET477 |
| A | PHE485 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GLY B 2001 |
| Chain | Residue |
| B | ARG526 |
| B | PHE2002 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PHE B 2002 |
| Chain | Residue |
| B | GLY368 |
| B | GLY369 |
| B | SER445 |
| B | TYR446 |
| B | PHE485 |
| B | ARG526 |
| B | THR527 |
| B | GLY2001 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 3001 |
| Chain | Residue |
| A | PRO151 |
| A | PHE170 |
| B | TYR478 |
| B | GLU490 |
| B | THR493 |
| B | GLY495 |
| B | ARG497 |
| B | MET500 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 3002 |
| Chain | Residue |
| B | ARG76 |
| B | LYS94 |
| B | LEU106 |
| B | GLU122 |
| B | LEU139 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 3003 |
| Chain | Residue |
| A | THR179 |
| A | SER180 |
| A | ASN181 |
| A | ARG188 |
| A | PRO225 |
| A | ARG226 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 3005 |
| Chain | Residue |
| A | ARG76 |
| A | LYS94 |
| A | LEU106 |
| A | GLU122 |
| A | ALA123 |
| A | LEU139 |
| A | ASP140 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1c4x |
| Chain | Residue | Details |
| A | SER445 | |
| A | HIS556 | |
| A | ASP524 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1c4x |
| Chain | Residue | Details |
| B | SER445 | |
| B | HIS556 | |
| B | ASP524 | |
