2QMW
The crystal structure of the prephenate dehydratase (PDT) from Staphylococcus aureus subsp. aureus Mu50
Replaces: 2IQ8Functional 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 |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 301 |
| Chain | Residue |
| A | ASN84 |
| A | PRO164 |
| A | HOH363 |
| A | HOH383 |
| A | HOH389 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT A 311 |
| Chain | Residue |
| A | TYR122 |
| A | ASP123 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 321 |
| Chain | Residue |
| A | THR168 |
| A | HOH337 |
| A | SER56 |
| A | ILE57 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 322 |
| Chain | Residue |
| A | THR206 |
| A | LEU209 |
| B | SER202 |
| B | THR206 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG A 331 |
| Chain | Residue |
| A | LEU6 |
| A | SER32 |
| A | ASN33 |
| A | LEU34 |
