Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004222 | molecular_function | metalloendopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 801 |
| Chain | Residue |
| A | ASP138 |
| A | GLU177 |
| A | ASP185 |
| A | GLU187 |
| A | GLU190 |
| A | HOH346 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 802 |
| Chain | Residue |
| A | GLU177 |
| A | ASN183 |
| A | ASP185 |
| A | GLU190 |
| A | HOH353 |
| A | HOH475 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 803 |
| Chain | Residue |
| A | ASP57 |
| A | ASP59 |
| A | GLN61 |
| A | HOH419 |
| A | HOH482 |
| A | HOH503 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 804 |
| Chain | Residue |
| A | TYR193 |
| A | THR194 |
| A | ILE197 |
| A | ASP200 |
| A | HOH354 |
| A | HOH480 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 805 |
| Chain | Residue |
| A | HIS142 |
| A | HIS146 |
| A | GLU166 |
| A | BZS807 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE DMS A 806 |
| Chain | Residue |
| A | SER218 |
| A | TYR251 |
| A | HOH506 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE BZS A 807 |
| Chain | Residue |
| A | ASN112 |
| A | ALA113 |
| A | VAL139 |
| A | HIS142 |
| A | GLU143 |
| A | HIS146 |
| A | TYR157 |
| A | GLU166 |
| A | ILE188 |
| A | LEU202 |
| A | ARG203 |
| A | HIS231 |
| A | HOH700 |
| A | HOH701 |
| A | HOH702 |
| A | ZN805 |
| site_id | BZS |
| Number of Residues | 7 |
| Details | |
| Chain | Residue |
| A | HIS231 |
| A | ASN112 |
| A | ZN805 |
| A | GLU143 |
| A | TYR157 |
| A | GLU166 |
| A | ARG203 |
| site_id | ZN |
| Number of Residues | 3 |
| Details | |
| Chain | Residue |
| A | GLU166 |
| A | HIS142 |
| A | HIS146 |
Functional Information from PROSITE/UniProt
| site_id | PS00142 |
| Number of Residues | 10 |
| Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VVAHELTHAV |
| Chain | Residue | Details |
| A | VAL139-VAL148 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"4808703","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"4808703","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1tlp |
| Chain | Residue | Details |
| A | HIS231 | |
| A | GLU143 | |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 176 |
| Chain | Residue | Details |
| A | HIS142 | metal ligand |
| A | GLU143 | electrostatic stabiliser, metal ligand |
| A | HIS146 | metal ligand |
| A | TYR157 | electrostatic stabiliser, hydrogen bond donor, steric role |
| A | GLU166 | metal ligand |
| A | ASP226 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| A | HIS231 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
