Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008236 | molecular_function | serine-type peptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 300 |
| Chain | Residue |
| A | ALA169 |
| A | TYR171 |
| A | VAL174 |
| A | HOH356 |
| A | HOH357 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 301 |
| Chain | Residue |
| A | GLN2 |
| A | ASP41 |
| A | LEU75 |
| A | ASN77 |
| A | THR79 |
| A | VAL81 |
| site_id | ACT |
| Number of Residues | 3 |
| Details | SERINE OF THE ACTIVE SITE HAS BEEN CHEMICALLY MODIFIED TO INCLUDE A COVALENT BOND FROM OG TO BORON OF THE INHIBITOR. |
| Chain | Residue |
| A | ASP32 |
| A | HIS64 |
| A | CLD221 |
| site_id | M1 |
| Number of Residues | 4 |
| Details | CALCIUM METAL BINDING SITE 1. |
| Chain | Residue |
| A | LEU75 |
| A | ASN77 |
| A | THR79 |
| A | VAL81 |
| site_id | M2 |
| Number of Residues | 2 |
| Details | CALCIUM METAL BINDING SITE 2. |
| Chain | Residue |
| A | ALA169 |
| A | VAL174 |
Functional Information from PROSITE/UniProt
| site_id | PS00136 |
| Number of Residues | 12 |
| Details | SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVLDTGIqasH |
| Chain | Residue | Details |
| A | VAL28-HIS39 | |
| site_id | PS00137 |
| Number of Residues | 11 |
| Details | SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGtVAA |
| Chain | Residue | Details |
| A | HIS64-ALA74 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | ASP32 | |
| A | HIS64 | |
| A | CLD221 | |
| Chain | Residue | Details |
| A | GLN2 | |
| A | ASP41 | |
| A | LEU75 | |
| A | ASN77 | |
| A | THR79 | |
| A | VAL81 | |
| A | ALA169 | |
| A | TYR171 | |
| A | VAL174 | |
