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 | 0009094 | biological_process | L-phenylalanine biosynthetic process |
A | 0016829 | molecular_function | lyase activity |
A | 0047769 | molecular_function | arogenate dehydratase 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 | 0047769 | molecular_function | arogenate dehydratase 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 |