Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004664 | molecular_function | prephenate dehydratase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| A | 0009094 | biological_process | L-phenylalanine biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016836 | molecular_function | hydro-lyase activity |
| B | 0004664 | molecular_function | prephenate dehydratase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| B | 0009094 | biological_process | L-phenylalanine biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016836 | molecular_function | hydro-lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT A 301 |
| Chain | Residue |
| A | ALA14 |
| A | TYR15 |
| A | SER16 |
| A | HOH315 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT A 302 |
| Chain | Residue |
| A | ARG263 |
| A | GLU264 |
| A | ALA266 |
| A | EDO308 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PHE A 303 |
| Chain | Residue |
| A | LEU225 |
| A | THR226 |
| A | LYS227 |
| B | ASN206 |
| B | GLU207 |
| B | GLY209 |
| B | SER210 |
| B | LEU211 |
| B | SER230 |
| B | TYR240 |
| A | ASP224 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PHE A 304 |
| Chain | Residue |
| A | ASN206 |
| A | GLU207 |
| A | GLY209 |
| A | SER210 |
| A | LEU211 |
| A | SER230 |
| A | TYR240 |
| B | ASP224 |
| B | LEU225 |
| B | THR226 |
| B | LYS227 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 306 |
| Chain | Residue |
| A | ARG195 |
| A | ASP224 |
| B | ASN206 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 307 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 308 |
| Chain | Residue |
| A | ARG263 |
| A | ALA266 |
| A | ACT302 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 309 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 310 |
| Chain | Residue |
| A | ARG221 |
| A | GLY222 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 311 |
| Chain | Residue |
| A | THR40 |
| A | GLU41 |
| A | GLN42 |
| B | PRO280 |
| site_id | BC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 312 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 281 |
| Chain | Residue |
| B | LYS98 |
| B | MSE100 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 282 |
| Chain | Residue |
| B | ILE223 |
| B | ASP224 |
| B | ILE247 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 283 |
| Chain | Residue |
| B | ARG263 |
| B | MSE268 |
| B | VAL269 |
Functional Information from PROSITE/UniProt
| site_id | PS00858 |
| Number of Residues | 8 |
| Details | PREPHENATE_DEHYDR_2 Prephenate dehydratase signature 2. LTKIESRP |
| Chain | Residue | Details |
| A | LEU225-PRO232 | |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 485 |
| Chain | Residue | Details |
| A | ASP183 | proton acceptor, proton donor |
| A | SER185 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 485 |
| Chain | Residue | Details |
| B | ASP183 | proton acceptor, proton donor |
| B | SER185 | electrostatic stabiliser |
