Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004222 | molecular_function | metalloendopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0031012 | cellular_component | extracellular matrix |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 996 |
| Chain | Residue |
| A | ASP137 |
| A | GLY169 |
| A | GLY171 |
| A | ASP173 |
| A | HOH397 |
| A | HOH402 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 997 |
| Chain | Residue |
| A | ILE159 |
| A | ASP177 |
| A | GLU180 |
| A | ASP154 |
| A | GLY155 |
| A | ASN157 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 998 |
| Chain | Residue |
| A | HIS147 |
| A | ASP149 |
| A | HIS162 |
| A | HIS175 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 999 |
| Chain | Residue |
| A | HIS197 |
| A | HIS201 |
| A | HIS207 |
| B | PAT3 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR CHAIN B OF THREE RESIDUE PEPTIDE INHIBITOR |
| Chain | Residue |
| A | SER151 |
| A | ALA161 |
| A | HIS162 |
| A | ALA163 |
| A | PHE164 |
| A | HIS197 |
| A | GLU198 |
| A | HIS201 |
| A | HIS207 |
| A | HOH329 |
| A | HOH394 |
| A | HOH420 |
| A | HOH555 |
| A | ZN999 |
| B | HOH478 |
| B | HOH500 |
| B | HOH512 |
Functional Information from PROSITE/UniProt
| site_id | PS00142 |
| Number of Residues | 10 |
| Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHEFGHSL |
| Chain | Residue | Details |
| A | VAL194-LEU203 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: |
| Chain | Residue | Details |
| A | GLU198 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP137 | |
| A | GLY169 | |
| A | GLY171 | |
| A | ASP173 | |
| Chain | Residue | Details |
| A | HIS147 | |
| A | GLU180 | |
| A | HIS197 | |
| A | HIS201 | |
| A | HIS207 | |
| A | ASP149 | |
| A | ASP154 | |
| A | GLY155 | |
| A | ASN157 | |
| A | ILE159 | |
| A | HIS162 | |
| A | HIS175 | |
| A | ASP177 | |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine |
| Chain | Residue | Details |
| A | ASN92 | |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN184 | |
| A | ASN226 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1hfs |
| Chain | Residue | Details |
| A | MET215 | |
| A | GLU198 | |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1hfs |
| Chain | Residue | Details |
| A | GLU198 | |
