Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
A | 0005829 | cellular_component | cytosol |
A | 0008652 | biological_process | amino acid biosynthetic process |
A | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
A | 0009423 | biological_process | chorismate biosynthetic process |
A | 0016829 | molecular_function | lyase activity |
A | 0019631 | biological_process | quinate catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 201 |
Chain | Residue |
A | SER54 |
A | SER54 |
A | SER54 |
A | HOH2173 |
A | HOH2173 |
A | HOH2174 |
A | HOH2174 |
A | HOH2174 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SO4 A 202 |
Chain | Residue |
A | GLU109 |
A | PHE111 |
A | ARG113 |
A | PRO119 |
A | HOH2175 |
A | HOH2176 |
A | HOH2177 |
A | HOH2178 |
A | HOH2179 |
A | HOH2184 |
A | ARG87 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 203 |
Chain | Residue |
A | TRP61 |
A | GLN64 |
A | HOH2094 |
A | HOH2180 |
A | HOH2181 |
site_id | AC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE FA6 A 200 |
Chain | Residue |
A | PRO11 |
A | LEU13 |
A | ARG19 |
A | ASN75 |
A | GLY77 |
A | GLY78 |
A | HIS81 |
A | ASP88 |
A | HIS101 |
A | ILE102 |
A | SER103 |
A | ARG112 |
A | HOH2172 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 204 |
Chain | Residue |
A | LEU128 |
A | GLY129 |
A | ILE130 |
A | GLN131 |
A | HIS143 |
A | HOH2182 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 205 |
Chain | Residue |
A | HIS81 |
A | HIS114 |
A | SER115 |
A | TYR116 |
A | HOH2151 |
A | HOH2177 |
A | HOH2184 |
A | HOH2185 |
A | HOH2186 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 206 |
Chain | Residue |
A | LYS46 |
A | ALA47 |
A | ARG50 |
Functional Information from PROSITE/UniProt
site_id | PS01029 |
Number of Residues | 18 |
Details | DEHYDROQUINASE_II Dehydroquinase class II signature. INGPNLgrLGrREpavYG |
Chain | Residue | Details |
A | ILE8-GLY25 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | TYR24 | |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor |
Chain | Residue | Details |
A | HIS101 | |
site_id | SWS_FT_FI3 |
Number of Residues | 5 |
Details | BINDING: |
Chain | Residue | Details |
A | ASN75 | |
A | HIS81 | |
A | ASP88 | |
A | ILE102 | |
A | ARG112 | |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
A | ARG19 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1uqr |
Chain | Residue | Details |
A | ARG19 | |
A | GLU99 | |
A | HIS101 | |
A | ASN12 | |
A | ARG108 | |