Functional Information from GO Data
Chain | GOid | namespace | contents |
E | 0004222 | molecular_function | metalloendopeptidase activity |
E | 0006508 | biological_process | proteolysis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue ZN E 401 |
Chain | Residue |
E | HIS142 |
E | HIS146 |
E | GLU166 |
E | 6NG409 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue CA E 402 |
Chain | Residue |
E | HOH589 |
E | ASP138 |
E | GLU177 |
E | ASP185 |
E | GLU187 |
E | GLU190 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue CA E 403 |
Chain | Residue |
E | ASP57 |
E | ASP59 |
E | GLN61 |
E | HOH602 |
E | HOH606 |
E | HOH807 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue CA E 404 |
Chain | Residue |
E | GLU177 |
E | ASN183 |
E | ASP185 |
E | GLU190 |
E | HOH569 |
E | HOH578 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue CA E 405 |
Chain | Residue |
E | TYR193 |
E | THR194 |
E | ILE197 |
E | ASP200 |
E | HOH612 |
E | HOH781 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue DMS E 406 |
Chain | Residue |
E | TYR66 |
E | HIS216 |
E | SER218 |
E | HOH894 |
E | HOH919 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue DMS E 407 |
Chain | Residue |
E | ILE1 |
E | THR2 |
E | GLY3 |
E | GLN31 |
E | ASN33 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue DMS E 408 |
Chain | Residue |
E | TYR110 |
E | PHE114 |
E | 6NG409 |
E | HOH509 |
site_id | AC9 |
Number of Residues | 15 |
Details | binding site for residue 6NG E 409 |
Chain | Residue |
E | ASN112 |
E | ALA113 |
E | PHE114 |
E | ASN116 |
E | HIS142 |
E | GLU143 |
E | HIS146 |
E | TYR157 |
E | GLU166 |
E | LEU202 |
E | ARG203 |
E | HIS231 |
E | ZN401 |
E | DMS408 |
E | HOH688 |
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 |
E | 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 | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 176 |