3WMX
GalE-like L-Threonine dehydrogenase from Cupriavidus necator (holo form)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0006567 | biological_process | L-threonine catabolic process |
| A | 0008743 | molecular_function | L-threonine 3-dehydrogenase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0006567 | biological_process | L-threonine catabolic process |
| B | 0008743 | molecular_function | L-threonine 3-dehydrogenase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0006567 | biological_process | L-threonine catabolic process |
| C | 0008743 | molecular_function | L-threonine 3-dehydrogenase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0006567 | biological_process | L-threonine catabolic process |
| D | 0008743 | molecular_function | L-threonine 3-dehydrogenase activity |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD A 401 |
| Chain | Residue |
| A | GLY12 |
| A | ALA55 |
| A | LEU76 |
| A | ALA77 |
| A | ALA78 |
| A | LEU94 |
| A | PRO117 |
| A | SER118 |
| A | SER119 |
| A | TYR144 |
| A | LYS148 |
| A | ASN14 |
| A | TYR171 |
| A | PRO172 |
| A | LEU174 |
| A | THR402 |
| A | HOH505 |
| A | HOH525 |
| A | HOH532 |
| B | VAL40 |
| B | PRO41 |
| B | THR42 |
| A | GLY15 |
| A | GLN16 |
| A | ILE17 |
| A | ASP38 |
| A | VAL39 |
| A | LEU53 |
| A | ASN54 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE THR A 402 |
| Chain | Residue |
| A | LEU80 |
| A | SER81 |
| A | SER119 |
| A | TYR144 |
| A | GLY184 |
| A | THR185 |
| A | THR186 |
| A | TRP280 |
| A | NAD401 |
| site_id | AC3 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD B 401 |
| Chain | Residue |
| A | VAL40 |
| A | PRO41 |
| A | THR42 |
| B | GLY12 |
| B | ASN14 |
| B | GLY15 |
| B | GLN16 |
| B | ILE17 |
| B | ASP38 |
| B | VAL39 |
| B | LEU53 |
| B | ASN54 |
| B | ALA55 |
| B | LEU76 |
| B | ALA77 |
| B | ALA78 |
| B | PRO117 |
| B | SER118 |
| B | SER119 |
| B | TYR144 |
| B | LYS148 |
| B | TYR171 |
| B | PRO172 |
| B | LEU174 |
| B | THR402 |
| B | HOH504 |
| B | HOH514 |
| B | HOH515 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE THR B 402 |
| Chain | Residue |
| B | LEU80 |
| B | SER81 |
| B | SER119 |
| B | TYR144 |
| B | GLY184 |
| B | THR185 |
| B | THR186 |
| B | NAD401 |
| site_id | AC5 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAD C 401 |
| Chain | Residue |
| C | GLY12 |
| C | ASN14 |
| C | GLY15 |
| C | GLN16 |
| C | ILE17 |
| C | ASP38 |
| C | VAL39 |
| C | LEU53 |
| C | ASN54 |
| C | ALA55 |
| C | LEU76 |
| C | ALA77 |
| C | ALA78 |
| C | LEU94 |
| C | PRO117 |
| C | SER118 |
| C | SER119 |
| C | TYR144 |
| C | LYS148 |
| C | TYR171 |
| C | PRO172 |
| C | LEU174 |
| C | GLY182 |
| C | HOH508 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NAD D 401 |
| Chain | Residue |
| D | ASN14 |
| D | GLY15 |
| D | GLN16 |
| D | ILE17 |
| D | ASP38 |
| D | VAL39 |
| D | LEU53 |
| D | ASN54 |
| D | ALA55 |
| D | LEU76 |
| D | ALA78 |
| D | LEU94 |
| D | PRO117 |
| D | SER118 |
| D | SER119 |
| D | TYR144 |
| D | LYS148 |
| D | TYR171 |
| D | PRO172 |
| D | LEU174 |
| D | GLY12 |
