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 | 6 |
Details | BINDING SITE FOR RESIDUE CA E 317 |
Chain | Residue |
E | ASP138 |
E | GLU177 |
E | ASP185 |
E | GLU187 |
E | GLU190 |
E | HOH338 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA E 318 |
Chain | Residue |
E | GLU190 |
E | HOH345 |
E | HOH431 |
E | GLU177 |
E | ASN183 |
E | ASP185 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA E 319 |
Chain | Residue |
E | ASP57 |
E | ASP59 |
E | GLN61 |
E | HOH394 |
E | HOH438 |
E | HOH454 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA E 320 |
Chain | Residue |
E | TYR193 |
E | THR194 |
E | ILE197 |
E | ASP200 |
E | HOH346 |
E | HOH436 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN E 321 |
Chain | Residue |
E | HIS142 |
E | HIS146 |
E | TYR157 |
E | GLU166 |
E | 0FA322 |
site_id | AC6 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE 0FA E 322 |
Chain | Residue |
E | ASN112 |
E | ALA113 |
E | HIS142 |
E | GLU143 |
E | HIS146 |
E | TYR157 |
E | GLU166 |
E | LEU202 |
E | ARG203 |
E | HIS231 |
E | ZN321 |
E | HOH353 |
E | HOH380 |
E | HOH490 |
E | HOH491 |
site_id | S1 |
Number of Residues | 1 |
Details | ACTIVE SITE SUBSITE S1 |
site_id | S1P |
Number of Residues | 7 |
Details | ACTIVE SITE SUBSITE S1 PRIME |
Chain | Residue |
E | PHE130 |
E | LEU133 |
E | VAL139 |
E | ILE188 |
E | GLY189 |
E | VAL192 |
E | LEU202 |
site_id | S2 |
Number of Residues | 1 |
Details | ACTIVE SITE SUBSITE S2 |
site_id | S2P |
Number of Residues | 2 |
Details | ACTIVE SITE SUBSITE S2 PRIME |
Chain | Residue |
E | PHE130 |
E | LEU202 |
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
Chain | Residue | Details |
E | GLU143 | |
Chain | Residue | Details |
E | HIS231 | |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
E | ASP57 | |
E | ASP185 | |
E | GLU187 | |
E | GLU190 | |
E | TYR193 | |
E | THR194 | |
E | ILE197 | |
E | ASP200 | |
E | ASP59 | |
E | GLN61 | |
E | ASP138 | |
E | HIS142 | |
E | HIS146 | |
E | GLU166 | |
E | GLU177 | |
E | ASN183 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1tlp |
Chain | Residue | Details |
E | HIS231 | |
E | GLU143 | |
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 176 |
Chain | Residue | Details |
E | HIS142 | metal ligand |
E | GLU143 | electrostatic stabiliser, metal ligand |
E | HIS146 | metal ligand |
E | TYR157 | electrostatic stabiliser, hydrogen bond donor, steric role |
E | GLU166 | metal ligand |
E | ASP226 | activator, electrostatic stabiliser, hydrogen bond acceptor |
E | HIS231 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |