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 | L4Z411 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue CA E 402 |
Chain | Residue |
E | HOH564 |
E | GLU177 |
E | ASN183 |
E | ASP185 |
E | GLU190 |
E | HOH534 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue CA E 403 |
Chain | Residue |
E | TYR193 |
E | THR194 |
E | ILE197 |
E | ASP200 |
E | HOH577 |
E | HOH671 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue CA E 404 |
Chain | Residue |
E | ASP138 |
E | GLU177 |
E | ASP185 |
E | GLU187 |
E | GLU190 |
E | HOH553 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue CA E 405 |
Chain | Residue |
E | ASP57 |
E | ASP59 |
E | GLN61 |
E | HOH542 |
E | HOH582 |
E | HOH711 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue DMS E 406 |
Chain | Residue |
E | ASN112 |
E | HIS142 |
E | GLU143 |
E | ARG203 |
E | L4Z411 |
E | HOH527 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue DMS E 407 |
Chain | Residue |
E | GLY259 |
E | ARG260 |
E | ASP261 |
E | HOH511 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue DMS E 408 |
Chain | Residue |
E | GLY95 |
E | PRO184 |
E | ASP185 |
E | TRP186 |
E | HOH507 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue TRS E 409 |
Chain | Residue |
E | LEU202 |
E | ARG203 |
E | ASP213 |
E | HIS231 |
site_id | AD1 |
Number of Residues | 7 |
Details | binding site for residue 47J E 410 |
Chain | Residue |
E | ASN159 |
E | TYR221 |
E | THR222 |
E | GLY223 |
E | GLY228 |
E | ASN233 |
E | HOH540 |
site_id | AD2 |
Number of Residues | 12 |
Details | binding site for residue L4Z E 411 |
Chain | Residue |
E | TYR110 |
E | ASN112 |
E | ALA113 |
E | HIS142 |
E | GLU143 |
E | HIS146 |
E | TYR157 |
E | GLU166 |
E | HIS231 |
E | ZN401 |
E | DMS406 |
E | HOH667 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue IPA E 412 |
Chain | Residue |
E | TYR24 |
E | TYR24 |
E | SER25 |
E | TYR28 |
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 | 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 |