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 401 |
| Chain | Residue |
| A | ASP138 |
| A | GLU177 |
| A | ASP185 |
| A | GLU187 |
| A | GLU190 |
| A | HOH1320 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 402 |
| Chain | Residue |
| A | GLU190 |
| A | HOH1334 |
| A | HOH1345 |
| A | GLU177 |
| A | ASN183 |
| A | ASP185 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 403 |
| Chain | Residue |
| A | ASP57 |
| A | ASP59 |
| A | GLN61 |
| A | HOH1329 |
| A | HOH1331 |
| A | HOH1336 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 404 |
| Chain | Residue |
| A | TYR193 |
| A | THR194 |
| A | ILE197 |
| A | ASP200 |
| A | HOH1324 |
| A | HOH1366 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 405 |
| Chain | Residue |
| A | HIS142 |
| A | HIS146 |
| A | GLU166 |
| A | ALA1317 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PHQ A 317 |
| Chain | Residue |
| A | ASN112 |
| A | ALA113 |
| A | LEU133 |
| A | VAL139 |
| A | GLU143 |
| A | ILE188 |
| A | LEU202 |
| A | ALA1317 |
| A | HOH1411 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ALA A 1317 |
| Chain | Residue |
| A | ASN112 |
| A | ALA113 |
| A | HIS142 |
| A | GLU143 |
| A | HIS146 |
| A | TYR157 |
| A | GLU166 |
| A | HIS231 |
| A | PHQ317 |
| A | ZN405 |
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 |
