Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004106 | molecular_function | chorismate mutase activity |
A | 0004664 | molecular_function | prephenate dehydratase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0009094 | biological_process | L-phenylalanine biosynthetic process |
A | 0016829 | molecular_function | lyase activity |
A | 0016836 | molecular_function | hydro-lyase activity |
B | 0004106 | molecular_function | chorismate mutase activity |
B | 0004664 | molecular_function | prephenate dehydratase activity |
B | 0005737 | cellular_component | cytoplasm |
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 | |