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 317 |
Chain | Residue |
A | ASP138 |
A | GLU177 |
A | ASP185 |
A | GLU187 |
A | GLU190 |
A | HOH1470 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 318 |
Chain | Residue |
A | GLU190 |
A | HOH1673 |
A | HOH1675 |
A | GLU177 |
A | ASN183 |
A | ASP185 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 319 |
Chain | Residue |
A | ASP57 |
A | ASP59 |
A | GLN61 |
A | HOH1436 |
A | HOH1603 |
A | HOH1604 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 320 |
Chain | Residue |
A | TYR193 |
A | THR194 |
A | ILE197 |
A | ASP200 |
A | HOH1517 |
A | HOH1606 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 321 |
Chain | Residue |
A | HIS142 |
A | HIS146 |
A | GLU166 |
A | BYA322 |
site_id | AC6 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE BYA A 322 |
Chain | Residue |
A | ASN112 |
A | ALA113 |
A | PHE130 |
A | LEU133 |
A | VAL139 |
A | HIS142 |
A | GLU143 |
A | HIS146 |
A | TYR157 |
A | GLU166 |
A | LEU202 |
A | ARG203 |
A | HIS231 |
A | ZN321 |
A | HOH1676 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE DMS A 323 |
Chain | Residue |
A | TRP115 |
A | HIS146 |
A | ASP150 |
A | TYR157 |
A | HOH1676 |
A | HOH1677 |
A | HOH1680 |
A | HOH1683 |
site_id | AC8 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE GOL A 324 |
Chain | Residue |
A | THR152 |
A | GLY247 |
A | GLY248 |
A | VAL255 |
A | GLN273 |
A | LEU275 |
A | HOH1432 |
A | HOH1434 |
A | HOH1487 |
A | HOH1507 |
A | HOH1632 |
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 | 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 |