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 | 169 |
| Number of Residues | 1 |
| Details | MUTATION FROM GLY TO ALA AT RESIDUE 169. |
| site_id | 206 |
| Number of Residues | 1 |
| Details | MUTATION FROM GLN TO CYS AT RESIDUE 206. SOME UNKNOWN COMPOUND IS BOUND TO THE SG. |
| site_id | 217 |
| Number of Residues | 1 |
| Details | MUTATION FROM TYR TO LYS AT RESIDUE 217. |
| site_id | 218 |
| Number of Residues | 1 |
| Details | MUTATION FROM ASN TO SER AT RESIDUE 218. |
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 295 |
| Chain | Residue |
| A | GLN2 |
| A | ASP41 |
| A | LEU75 |
| A | ASN77 |
| A | ILE79 |
| A | VAL81 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 297 |
| Chain | Residue |
| A | GLU195 |
| A | ASP197 |
| A | HOH296 |
| A | HOH340 |
| A | HOH372 |
| A | HOH483 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNX A 277 |
| Chain | Residue |
| A | CYS206 |
| A | UNX278 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE UNX A 278 |
| Chain | Residue |
| A | CYS206 |
| A | GLY215 |
| A | UNX277 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE IPA A 290 |
| Chain | Residue |
| A | PHE58 |
| A | ARG186 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE IPA A 291 |
| Chain | Residue |
| A | SER145 |
| A | PHE189 |
| site_id | C22 |
| Number of Residues | 1 |
| Details | MUTATION FROM THR TO CYS AT RESIDUE 22. CYS 22 FORMS A DISULFIDE BOND WITH CYS 87. |
| site_id | C87 |
| Number of Residues | 1 |
| Details | MUTATION FROM SER TO CYS AT RESIDUE 87. CYS 87 FORMS A DISULFIDE BOND WITH CYS 22. |
| site_id | CA1 |
| Number of Residues | 1 |
| Details | HIGH AFFINITY CALCIUM BINDING SITE. |
| site_id | CA2 |
| Number of Residues | 1 |
| Details | LOW AFFINITY CALCIUM BINDING SITE. |
| site_id | F50 |
| Number of Residues | 1 |
| Details | MUTATION FROM MET TO PHE AT RESIDUE 50. |
Functional Information from PROSITE/UniProt
| site_id | PS00136 |
| Number of Residues | 12 |
| Details | SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVIDSGIdssH |
| 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 | |
| site_id | PS00138 |
| Number of Residues | 11 |
| Details | SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAsPhVAG |
| Chain | Residue | Details |
| A | GLY219-GLY229 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | ASP32 | |
| A | HIS64 | |
| A | SER221 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLN2 | |
| A | ASN77 | |
| A | ILE79 | |
| A | VAL81 | |
| A | ALA169 | |
| A | TYR171 | |
| A | VAL174 | |
| A | ASP41 | |
| A | LEU75 | |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 723 |
| Chain | Residue | Details |
| A | ASP32 | electrostatic interaction, electrostatic stabiliser |
| A | HIS64 | proton acceptor, proton donor |
| A | ASN155 | electrostatic interaction, electrostatic stabiliser |
| A | SER221 | nucleofuge, nucleophile, proton acceptor, proton donor |
