4YWJ
Crystal structure of 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) from Pseudomonas aeruginosa
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| 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 | 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 | 26 |
| Details | binding site for residue NAD A 300 |
| Chain | Residue |
| A | VAL7 |
| A | VAL81 |
| A | GLY99 |
| A | THR101 |
| A | ALA123 |
| A | ALA124 |
| A | ASN125 |
| A | PHE126 |
| A | ARG237 |
| A | PHE240 |
| A | PGE301 |
| A | ALA10 |
| A | HOH412 |
| A | HOH423 |
| A | HOH431 |
| A | HOH452 |
| A | HOH462 |
| A | HOH478 |
| A | HOH499 |
| A | GLY11 |
| A | ARG12 |
| A | MET13 |
| A | ASP35 |
| A | ARG36 |
| A | PHE76 |
| A | THR77 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue PGE A 301 |
| Chain | Residue |
| A | THR101 |
| A | ALA124 |
| A | ASN125 |
| A | PHE240 |
| A | NAD300 |
| A | HOH430 |
| A | HOH454 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue BU1 A 302 |
| Chain | Residue |
| A | ILE153 |
| A | THR218 |
| A | HOH415 |
| A | HOH500 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 303 |
| Chain | Residue |
| A | THR139 |
| B | THR139 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | binding site for residue NAD B 300 |
| Chain | Residue |
| B | VAL7 |
| B | GLY8 |
| B | ALA10 |
| B | GLY11 |
| B | ARG12 |
| B | MET13 |
| B | ASP35 |
| B | ARG36 |
| B | PHE76 |
| B | THR77 |
| B | VAL81 |
| B | GLY99 |
| B | THR101 |
| B | ALA123 |
| B | ALA124 |
| B | ASN125 |
| B | PHE126 |
| B | ARG237 |
| B | PHE240 |
| B | PGE301 |
| B | HOH415 |
| B | HOH467 |
| B | HOH469 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue PGE B 301 |
| Chain | Residue |
| B | ASN125 |
| B | PHE240 |
| B | NAD300 |
| B | HOH413 |
| B | HOH505 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue BU1 B 302 |
| Chain | Residue |
| B | ILE153 |
| B | ASP216 |
| B | HIS217 |
| B | THR218 |
| B | HOH416 |
| B | HOH417 |
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 | GLY8 | |
| B | ARG36 | |
| B | GLY99 | |
| B | ALA123 | |
| B | HIS157 | |
| B | GLY166 | |
| A | ASP35 | |
| A | ARG36 | |
| A | GLY99 | |
| A | ALA123 | |
| A | HIS157 | |
| A | GLY166 | |
| B | GLY8 | |
| B | ASP35 |
