Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
| 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 | 12 |
| Details | binding site for residue ETE A 201 |
| Chain | Residue |
| A | GLY-2 |
| A | HOH459 |
| A | HOH467 |
| A | HOH529 |
| A | GLU118 |
| A | PRO119 |
| A | VAL120 |
| A | GOL206 |
| A | HOH328 |
| A | HOH331 |
| A | HOH357 |
| A | HOH364 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue SER A 202 |
| Chain | Residue |
| A | TYR64 |
| A | PHE65 |
| A | ASN66 |
| A | GLY67 |
| A | ASN106 |
| A | GLN124 |
| A | VAL126 |
| A | HOH384 |
| A | HOH521 |
| A | HOH577 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue FLC A 205 |
| Chain | Residue |
| A | LEU11 |
| A | ARG17 |
| A | TYR22 |
| A | ASN74 |
| A | GLY76 |
| A | ALA77 |
| A | HIS80 |
| A | HIS101 |
| A | ILE102 |
| A | SER103 |
| A | VAL105 |
| A | ARG112 |
| A | HOH349 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 206 |
| Chain | Residue |
| A | ARG17 |
| A | GLU18 |
| A | TYR22 |
| A | ASP87 |
| A | ALA90 |
| A | SER91 |
| A | ARG112 |
| A | ETE201 |
| A | HOH304 |
| A | HOH331 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | binding site for residues SO4 A 203 and SO4 A 204 |
| Chain | Residue |
| A | HIS52 |
| A | HIS52 |
| A | HIS52 |
| A | GLU53 |
| A | GLU53 |
| A | GLU53 |
| A | GLY54 |
| A | GLY54 |
| A | GLY54 |
| A | HOH302 |
| A | HOH302 |
| A | HOH302 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | binding site for residues SO4 A 203 and SO4 A 204 |
| Chain | Residue |
| A | HIS52 |
| A | HIS52 |
| A | HIS52 |
| A | GLU53 |
| A | GLU53 |
| A | GLU53 |
| A | GLY54 |
| A | GLY54 |
| A | GLY54 |
| A | HOH302 |
| A | HOH302 |
| A | HOH302 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | binding site for residues SO4 A 203 and SO4 A 204 |
| Chain | Residue |
| A | HIS52 |
| A | HIS52 |
| A | HIS52 |
| A | GLU53 |
| A | GLU53 |
| A | GLU53 |
| A | GLY54 |
| A | GLY54 |
| A | GLY54 |
| A | HOH302 |
| A | HOH302 |
| A | HOH302 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | binding site for residues SO4 A 203 and SO4 A 204 |
| Chain | Residue |
| A | HIS52 |
| A | HIS52 |
| A | HIS52 |
| A | GLU53 |
| A | GLU53 |
| A | GLU53 |
| A | GLY54 |
| A | GLY54 |
| A | GLY54 |
| A | HOH302 |
| A | HOH302 |
| A | HOH302 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | binding site for residues SO4 A 203 and SO4 A 204 |
| Chain | Residue |
| A | GLY54 |
| A | GLY54 |
| A | GLY54 |
| A | HOH302 |
| A | HOH302 |
| A | HOH302 |
| A | HIS52 |
| A | HIS52 |
| A | HIS52 |
| A | GLU53 |
| A | GLU53 |
| A | GLU53 |
| site_id | AD1 |
| Number of Residues | 12 |
| Details | binding site for residues SO4 A 203 and SO4 A 204 |
| Chain | Residue |
| A | HIS52 |
| A | HIS52 |
| A | HIS52 |
| A | GLU53 |
| A | GLU53 |
| A | GLU53 |
| A | GLY54 |
| A | GLY54 |
| A | GLY54 |
| A | HOH302 |
| A | HOH302 |
| A | HOH302 |
Functional Information from PROSITE/UniProt
| site_id | PS01029 |
| Number of Residues | 18 |
| Details | DEHYDROQUINASE_II Dehydroquinase class II signature. INGPNLnfLGiREkniYG |
| Chain | Residue | Details |
| A | ILE6-GLY23 | |
