6VH5
Crystal structure of prephenate dehydratase from brucella melitensis biovar abortus 2308 in complex with phenylalanine
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 |
| C | 0004664 | molecular_function | prephenate dehydratase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| C | 0009094 | biological_process | L-phenylalanine biosynthetic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016836 | molecular_function | hydro-lyase activity |
| D | 0004664 | molecular_function | prephenate dehydratase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008652 | biological_process | amino acid biosynthetic process |
| D | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| D | 0009094 | biological_process | L-phenylalanine biosynthetic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016836 | molecular_function | hydro-lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue PHE A 301 |
| Chain | Residue |
| A | ASN222 |
| C | THR238 |
| C | PHE240 |
| C | EDO302 |
| A | MET223 |
| A | THR224 |
| A | LYS225 |
| C | ASN204 |
| C | VAL205 |
| C | ALA207 |
| C | ALA208 |
| C | LEU209 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| A | ALA207 |
| A | LEU209 |
| A | TYR210 |
| C | PHE216 |
| C | VAL221 |
| C | PHE301 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | binding site for residue PHE B 301 |
| Chain | Residue |
| B | ASN222 |
| B | MET223 |
| B | THR224 |
| B | LYS225 |
| D | ASN204 |
| D | VAL205 |
| D | ALA208 |
| D | LEU209 |
| D | SER228 |
| D | THR238 |
| D | PHE240 |
| D | EDO302 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 302 |
| Chain | Residue |
| B | ALA207 |
| B | ALA208 |
| B | LEU209 |
| B | TYR210 |
| D | PHE216 |
| D | VAL221 |
| D | PHE301 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 303 |
| Chain | Residue |
| B | LEU109 |
| B | GLY123 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | binding site for residue PHE C 301 |
| Chain | Residue |
| A | ASN204 |
| A | VAL205 |
| A | ALA207 |
| A | ALA208 |
| A | LEU209 |
| A | THR238 |
| A | PHE240 |
| A | EDO302 |
| C | ASN222 |
| C | MET223 |
| C | THR224 |
| C | LYS225 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue EDO C 302 |
| Chain | Residue |
| A | PHE216 |
| A | VAL221 |
| A | PHE301 |
| C | ALA207 |
| C | ALA208 |
| C | LEU209 |
| C | TYR210 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | binding site for residue PHE D 301 |
| Chain | Residue |
| B | ASN204 |
| B | VAL205 |
| B | ALA207 |
| B | ALA208 |
| B | LEU209 |
| B | THR238 |
| B | PHE240 |
| B | EDO302 |
| D | ASN222 |
| D | MET223 |
| D | THR224 |
| D | LYS225 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue EDO D 302 |
| Chain | Residue |
| B | PHE216 |
| B | ALA217 |
| B | VAL221 |
| B | PHE301 |
| D | ALA207 |
| D | ALA208 |
| D | LEU209 |
| D | TYR210 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 303 |
| Chain | Residue |
| D | HIS66 |
| D | TYR229 |
| D | LEU231 |
| D | GLN239 |
| D | HOH416 |
Functional Information from PROSITE/UniProt
| site_id | PS00857 |
| Number of Residues | 23 |
| Details | PREPHENATE_DEHYDR_1 Prephenate dehydratase signature 1. YgLdiLeenveDsennvTRFVvL |
| Chain | Residue | Details |
| A | TYR156-LEU178 |
