7MQV
Crystal structure of truncated (ACT domain removed) prephenate dehydrogenase tyrA from Bacillus anthracis in complex with NAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004665 | molecular_function | prephenate dehydrogenase (NADP+) activity |
| A | 0006571 | biological_process | L-tyrosine biosynthetic process |
| A | 0008977 | molecular_function | prephenate dehydrogenase (NAD+) activity |
| A | 0070403 | molecular_function | NAD+ binding |
| B | 0004665 | molecular_function | prephenate dehydrogenase (NADP+) activity |
| B | 0006571 | biological_process | L-tyrosine biosynthetic process |
| B | 0008977 | molecular_function | prephenate dehydrogenase (NAD+) activity |
| B | 0070403 | molecular_function | NAD+ binding |
| C | 0004665 | molecular_function | prephenate dehydrogenase (NADP+) activity |
| C | 0006571 | biological_process | L-tyrosine biosynthetic process |
| C | 0008977 | molecular_function | prephenate dehydrogenase (NAD+) activity |
| C | 0070403 | molecular_function | NAD+ binding |
| D | 0004665 | molecular_function | prephenate dehydrogenase (NADP+) activity |
| D | 0006571 | biological_process | L-tyrosine biosynthetic process |
| D | 0008977 | molecular_function | prephenate dehydrogenase (NAD+) activity |
| D | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | binding site for residue NAD A 401 |
| Chain | Residue |
| A | GLY21 |
| A | PRO82 |
| A | VAL83 |
| A | GLU85 |
| A | VAL107 |
| A | GLY108 |
| A | SER109 |
| A | PRO133 |
| A | ALA135 |
| A | GLY136 |
| A | SER137 |
| A | GLY23 |
| A | THR140 |
| A | GLY141 |
| A | MET243 |
| A | HOH504 |
| A | HOH515 |
| A | HOH538 |
| A | LEU24 |
| A | ILE25 |
| A | ASP45 |
| A | ILE46 |
| A | GLN50 |
| A | ALA80 |
| A | SER81 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | binding site for residue NAD B 401 |
| Chain | Residue |
| B | GLY21 |
| B | GLY23 |
| B | LEU24 |
| B | ILE25 |
| B | ASP45 |
| B | ILE46 |
| B | PHE47 |
| B | GLN50 |
| B | ALA80 |
| B | SER81 |
| B | PRO82 |
| B | GLU85 |
| B | LEU89 |
| B | VAL107 |
| B | GLY108 |
| B | SER109 |
| B | PRO133 |
| B | ALA135 |
| B | MET243 |
| B | HOH509 |
| B | HOH517 |
| B | HOH520 |
| B | HOH523 |
| site_id | AC3 |
| Number of Residues | 28 |
| Details | binding site for residue NAD C 401 |
| Chain | Residue |
| C | GLY21 |
| C | GLY23 |
| C | LEU24 |
| C | ILE25 |
| C | ASP45 |
| C | ILE46 |
| C | GLN50 |
| C | ALA80 |
| C | SER81 |
| C | PRO82 |
| C | VAL83 |
| C | GLU85 |
| C | LEU89 |
| C | VAL107 |
| C | GLY108 |
| C | SER109 |
| C | PRO133 |
| C | ALA135 |
| C | GLY136 |
| C | SER137 |
| C | THR140 |
| C | GLY141 |
| C | MET243 |
| C | HOH501 |
| C | HOH511 |
| C | HOH521 |
| C | HOH522 |
| C | HOH526 |
| site_id | AC4 |
| Number of Residues | 29 |
| Details | binding site for residue NAD D 401 |
| Chain | Residue |
| D | GOL402 |
| D | HOH511 |
| D | HOH518 |
| D | HOH532 |
| D | HOH537 |
| D | HOH546 |
| D | GLY23 |
| D | LEU24 |
| D | ILE25 |
| D | ASP45 |
| D | ILE46 |
| D | PHE47 |
| D | GLN50 |
| D | ALA80 |
| D | SER81 |
| D | PRO82 |
| D | VAL83 |
| D | GLU85 |
| D | LEU89 |
| D | VAL107 |
| D | GLY108 |
| D | SER109 |
| D | PRO133 |
| D | ALA135 |
| D | GLY136 |
| D | SER137 |
| D | THR140 |
| D | GLY141 |
| D | MET243 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue GOL D 402 |
| Chain | Residue |
| D | SER109 |
| D | HIS132 |
| D | MET134 |
| D | SER198 |
| D | HIS202 |
| D | NAD401 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue CL D 403 |
| Chain | Residue |
| D | PHE154 |
| D | ARG300 |
