Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0004181 | molecular_function | metallocarboxypeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0008270 | molecular_function | zinc ion binding |
| C | 0004252 | molecular_function | serine-type endopeptidase activity |
| C | 0005576 | cellular_component | extracellular region |
| C | 0005615 | cellular_component | extracellular space |
| C | 0006508 | biological_process | proteolysis |
| C | 0007586 | biological_process | digestion |
| D | 0004252 | molecular_function | serine-type endopeptidase activity |
| D | 0005576 | cellular_component | extracellular region |
| D | 0005615 | cellular_component | extracellular space |
| D | 0006508 | biological_process | proteolysis |
| D | 0008236 | molecular_function | serine-type peptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA C 650 |
| Chain | Residue |
| C | GLU470 |
| C | ASP472 |
| C | VAL475 |
| C | GLN477 |
| C | GLU480 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 350 |
| Chain | Residue |
| B | HIS69 |
| B | GLU72 |
| B | HIS196 |
| B | HOH351 |
Functional Information from PROSITE/UniProt
| site_id | PS00132 |
| Number of Residues | 23 |
| Details | CARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PaIwIdlGiHSrEwITQatgvwF |
| Chain | Residue | Details |
| B | PRO60-PHE82 | |
| site_id | PS00133 |
| Number of Residues | 11 |
| Details | CARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HSYSQLLlYPY |
| Chain | Residue | Details |
| B | HIS196-TYR206 | |
| site_id | PS00134 |
| Number of Residues | 6 |
| Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAGHC |
| Chain | Residue | Details |
| C | VAL453-CYS458 | |
| D | LEU753-CYS758 | |
| site_id | PS00135 |
| Number of Residues | 12 |
| Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. SGcdGDSGGPLN |
| Chain | Residue | Details |
| C | SER589-ASN600 | |
| D | SER889-ASN900 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: Charge relay system => ECO:0000250 |
| Chain | Residue | Details |
| D | HIS757 | |
| D | ASP802 | |
| D | SER895 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| D | ASN709 | |
| B | GLU72 | |
| B | HIS196 | |
| Chain | Residue | Details |
| B | ARG127 | |
| B | ASN144 | |
| B | SER197 | |
| B | TYR248 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| D | HIS757 | |
| D | ASP802 | |
| D | SER895 | |
| site_id | CSA10 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| C | SER595 | |
| C | GLY593 | |
| C | HIS457 | |
| C | SER614 | |
| C | ASP502 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| C | SER595 | |
| C | HIS457 | |
| C | ASP502 | |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| B | ARG127 | |
| B | GLU270 | |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| B | ARG71 | |
| B | GLU270 | |
| B | ARG127 | |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| C | SER595 | |
| C | GLY593 | |
| C | HIS457 | |
| C | ASP502 | |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| D | GLY893 | |
| D | HIS757 | |
| D | ASP802 | |
| D | SER895 | |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| C | SER595 | |
| C | HIS457 | |
| C | GLY596 | |
| C | ASP502 | |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| D | HIS757 | |
| D | ASP802 | |
| D | GLY896 | |
| D | SER895 | |
| site_id | CSA9 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| D | GLY893 | |
| D | HIS757 | |
| D | SER914 | |
| D | ASP786 | |
| D | SER895 | |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 171 |
| Chain | Residue | Details |
| B | HIS69 | metal ligand |
| B | GLU72 | metal ligand |
| B | ARG127 | electrostatic stabiliser, hydrogen bond donor |
| B | HIS196 | metal ligand |
| B | GLU270 | covalently attached, electrofuge, electrophile, hydrogen bond acceptor, hydrogen bond donor, nucleophile, proton acceptor, proton donor |
