4K28
2.15 Angstrom resolution crystal structure of a shikimate dehydrogenase family protein from Pseudomonas putida KT2440 in complex with NAD+
Replaces: 3TUMFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004764 | molecular_function | shikimate 3-dehydrogenase (NADP+) activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0009423 | biological_process | chorismate biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019632 | biological_process | shikimate metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050661 | molecular_function | NADP binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004764 | molecular_function | shikimate 3-dehydrogenase (NADP+) activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0009423 | biological_process | chorismate biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019632 | biological_process | shikimate metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAD A 301 |
| Chain | Residue |
| A | ILE131 |
| A | ALA194 |
| A | SER195 |
| A | PRO196 |
| A | MET199 |
| A | VAL224 |
| A | GLY247 |
| A | MET250 |
| A | ALA251 |
| A | GLN254 |
| A | HOH403 |
| A | GLY132 |
| A | HOH501 |
| A | HOH520 |
| A | HOH531 |
| A | HOH533 |
| A | GLY134 |
| A | GLY135 |
| A | VAL136 |
| A | CYS155 |
| A | ASP156 |
| A | PRO157 |
| A | ARG161 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MN A 302 |
| Chain | Residue |
| A | CYS155 |
| A | PHE182 |
| A | LEU207 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MN A 303 |
| Chain | Residue |
| A | CYS166 |
| A | VAL178 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MN A 304 |
| Chain | Residue |
| A | CYS34 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAD B 301 |
| Chain | Residue |
| B | ILE131 |
| B | GLY132 |
| B | GLY134 |
| B | GLY135 |
| B | VAL136 |
| B | CYS155 |
| B | ASP156 |
| B | PRO157 |
| B | ARG161 |
| B | ALA194 |
| B | SER195 |
| B | PRO196 |
| B | MET199 |
| B | VAL224 |
| B | THR226 |
| B | GLY247 |
| B | ALA251 |
| B | GLN254 |
| B | HOH428 |
| B | HOH445 |
| B | HOH491 |
| B | HOH511 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA B 302 |
| Chain | Residue |
| B | VAL68 |
| B | PRO69 |
| B | TYR70 |
| B | LYS71 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MN B 303 |
| Chain | Residue |
| B | CYS34 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MN B 304 |
| Chain | Residue |
| B | CYS155 |
| B | PHE182 |
| B | LEU207 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MN B 305 |
| Chain | Residue |
| B | CYS166 |
| B | VAL178 |
