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 | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 501 |
| Chain | Residue |
| A | HIS142 |
| A | HIS146 |
| A | GLU166 |
| A | HOH510 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 502 |
| Chain | Residue |
| A | HOH522 |
| A | ASP138 |
| A | GLU177 |
| A | ASP185 |
| A | GLU187 |
| A | GLU190 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 503 |
| Chain | Residue |
| A | GLU177 |
| A | ASN183 |
| A | ASP185 |
| A | GLU190 |
| A | HOH521 |
| A | HOH538 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 504 |
| Chain | Residue |
| A | ASP57 |
| A | ASP59 |
| A | GLN61 |
| A | HOH524 |
| A | HOH535 |
| A | HOH555 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 505 |
| Chain | Residue |
| A | TYR193 |
| A | THR194 |
| A | ILE197 |
| A | ASP200 |
| A | HOH546 |
| A | HOH573 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE DMS A 506 |
| Chain | Residue |
| A | HIS216 |
| A | SER218 |
| A | TYR251 |
| A | HOH617 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE IPH A 507 |
| Chain | Residue |
| A | LEU133 |
| A | VAL139 |
| A | HIS142 |
| A | GLU143 |
| A | LEU202 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE IPH A 508 |
| Chain | Residue |
| A | TYR84 |
| A | SER92 |
| A | TYR93 |
| A | ILE100 |
| A | LEU144 |
| A | VAL148 |
| A | HOH529 |
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 |
