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 1317 |
Chain | Residue |
A | HIS142 |
A | HIS146 |
A | GLU166 |
A | HOH2189 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 1318 |
Chain | Residue |
A | HOH2188 |
A | ASP138 |
A | GLU177 |
A | ASP185 |
A | GLU187 |
A | GLU190 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 1319 |
Chain | Residue |
A | GLU177 |
A | ASN183 |
A | ASP185 |
A | GLU190 |
A | HOH2211 |
A | HOH2214 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 1320 |
Chain | Residue |
A | ASP57 |
A | ASP59 |
A | GLN61 |
A | HOH2095 |
A | HOH2096 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 1321 |
Chain | Residue |
A | TYR193 |
A | THR194 |
A | ILE197 |
A | ASP200 |
A | HOH2220 |
A | HOH2222 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DMS A 1324 |
Chain | Residue |
A | TYR66 |
A | HIS216 |
A | SER218 |
A | TYR251 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE TMO A 1325 |
Chain | Residue |
A | LEU50 |
A | TYR93 |
A | GLY117 |
A | SER118 |
A | TYR151 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE TMO A 1326 |
Chain | Residue |
A | TYR151 |
A | SER206 |
A | LYS239 |
A | HOH2143 |
A | HOH2232 |
A | HOH2235 |
site_id | AC9 |
Number of Residues | 11 |
Details | Binding site for Di-peptide VAL A1322 and LYS A1323 |
Chain | Residue |
A | ASN111 |
A | ASN112 |
A | ALA113 |
A | PHE130 |
A | GLU143 |
A | ARG203 |
A | HIS231 |
A | HOH2189 |
A | HOH2254 |
A | HOH2325 |
A | HOH2326 |
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
Chain | Residue | Details |
A | GLU143 | |
Chain | Residue | Details |
A | HIS231 | |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP57 | |
A | ASP185 | |
A | GLU187 | |
A | GLU190 | |
A | TYR193 | |
A | THR194 | |
A | ILE197 | |
A | ASP200 | |
A | ASP59 | |
A | GLN61 | |
A | ASP138 | |
A | HIS142 | |
A | HIS146 | |
A | GLU166 | |
A | GLU177 | |
A | ASN183 | |
Catalytic Information from CSA
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 |