4F3Y
X-Ray Crystal Structure of Dihydrodipicolinate reductase from Burkholderia thailandensis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase |
| A | 0009085 | biological_process | lysine biosynthetic process |
| A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016726 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor |
| A | 0019877 | biological_process | diaminopimelate biosynthetic process |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051287 | molecular_function | NAD binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase |
| B | 0009085 | biological_process | lysine biosynthetic process |
| B | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016726 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor |
| B | 0019877 | biological_process | diaminopimelate biosynthetic process |
| B | 0050661 | molecular_function | NADP binding |
| B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 301 |
| Chain | Residue |
| A | VAL23 |
| A | LEU24 |
| A | ALA26 |
| A | ALA29 |
| A | HOH518 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 302 |
| Chain | Residue |
| A | ARG191 |
| A | HOH459 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA B 301 |
| Chain | Residue |
| B | THR179 |
| B | ARG181 |
| B | ILE175 |
| B | ALA176 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 302 |
| Chain | Residue |
| B | VAL23 |
| B | LEU24 |
| B | ALA26 |
| B | ALA29 |
| B | HOH458 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 303 |
| Chain | Residue |
| B | GLY10 |
| B | ASP36 |
| B | HIS85 |
Functional Information from PROSITE/UniProt
| site_id | PS01298 |
| Number of Residues | 18 |
| Details | DAPB Dihydrodipicolinate reductase signature. EIiEaHhrhKvDapSGTA |
| Chain | Residue | Details |
| A | GLU151-ALA168 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00102 |
| Chain | Residue | Details |
| A | HIS156 | |
| B | HIS156 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00102 |
| Chain | Residue | Details |
| A | LYS160 | |
| B | LYS160 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00102 |
| Chain | Residue | Details |
| A | GLY10 | |
| B | ARG37 | |
| B | GLY99 | |
| B | SER123 | |
| B | HIS157 | |
| B | GLY166 | |
| A | ASP36 | |
| A | ARG37 | |
| A | GLY99 | |
| A | SER123 | |
| A | HIS157 | |
| A | GLY166 | |
| B | GLY10 | |
| B | ASP36 |
