3OET
D-Erythronate-4-Phosphate Dehydrogenase complexed with NAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008615 | biological_process | pyridoxine biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0033711 | molecular_function | 4-phosphoerythronate dehydrogenase activity |
| A | 0036001 | biological_process | 'de novo' pyridoxal 5'-phosphate biosynthetic process |
| A | 0046983 | molecular_function | protein dimerization activity |
| A | 0051287 | molecular_function | NAD binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008615 | biological_process | pyridoxine biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0033711 | molecular_function | 4-phosphoerythronate dehydrogenase activity |
| B | 0036001 | biological_process | 'de novo' pyridoxal 5'-phosphate biosynthetic process |
| B | 0046983 | molecular_function | protein dimerization activity |
| B | 0051287 | molecular_function | NAD binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0008615 | biological_process | pyridoxine biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0033711 | molecular_function | 4-phosphoerythronate dehydrogenase activity |
| C | 0036001 | biological_process | 'de novo' pyridoxal 5'-phosphate biosynthetic process |
| C | 0046983 | molecular_function | protein dimerization activity |
| C | 0051287 | molecular_function | NAD binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0008615 | biological_process | pyridoxine biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0033711 | molecular_function | 4-phosphoerythronate dehydrogenase activity |
| D | 0036001 | biological_process | 'de novo' pyridoxal 5'-phosphate biosynthetic process |
| D | 0046983 | molecular_function | protein dimerization activity |
| D | 0051287 | molecular_function | NAD binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005829 | cellular_component | cytosol |
| E | 0008615 | biological_process | pyridoxine biosynthetic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| E | 0033711 | molecular_function | 4-phosphoerythronate dehydrogenase activity |
| E | 0036001 | biological_process | 'de novo' pyridoxal 5'-phosphate biosynthetic process |
| E | 0046983 | molecular_function | protein dimerization activity |
| E | 0051287 | molecular_function | NAD binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0005829 | cellular_component | cytosol |
| F | 0008615 | biological_process | pyridoxine biosynthetic process |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| F | 0033711 | molecular_function | 4-phosphoerythronate dehydrogenase activity |
| F | 0036001 | biological_process | 'de novo' pyridoxal 5'-phosphate biosynthetic process |
| F | 0046983 | molecular_function | protein dimerization activity |
| F | 0051287 | molecular_function | NAD binding |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0005829 | cellular_component | cytosol |
| G | 0008615 | biological_process | pyridoxine biosynthetic process |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| G | 0033711 | molecular_function | 4-phosphoerythronate dehydrogenase activity |
| G | 0036001 | biological_process | 'de novo' pyridoxal 5'-phosphate biosynthetic process |
| G | 0046983 | molecular_function | protein dimerization activity |
| G | 0051287 | molecular_function | NAD binding |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0005829 | cellular_component | cytosol |
| H | 0008615 | biological_process | pyridoxine biosynthetic process |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| H | 0033711 | molecular_function | 4-phosphoerythronate dehydrogenase activity |
| H | 0036001 | biological_process | 'de novo' pyridoxal 5'-phosphate biosynthetic process |
| H | 0046983 | molecular_function | protein dimerization activity |
| H | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD A 379 |
| Chain | Residue |
| A | ASN91 |
| A | PRO148 |
| A | HIS174 |
| A | THR175 |
| A | PRO176 |
| A | TYR183 |
| A | THR185 |
| A | ALA206 |
| A | CYS207 |
| A | ARG208 |
| A | ASP232 |
| A | VAL95 |
| A | HIS254 |
| A | ALA256 |
| A | GLY257 |
| A | HOH382 |
| A | HOH394 |
| A | HOH401 |
| A | HOH411 |
| A | HOH422 |
| A | GLY123 |
| A | GLY125 |
| A | ASN126 |
| A | VAL127 |
| A | CYS145 |
| A | ASP146 |
| A | PRO147 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAD B 379 |
| Chain | Residue |
| B | ASN91 |
| B | VAL95 |
| B | GLY123 |
| B | GLY125 |
| B | ASN126 |
| B | VAL127 |
| B | ASP146 |
| B | PRO147 |
| B | PRO148 |
| B | HIS174 |
| B | THR175 |
| B | PRO176 |
| B | TYR183 |
| B | THR185 |
| B | ALA206 |
| B | CYS207 |
| B | ARG208 |
| B | ASP232 |
| B | HIS254 |
| B | ALA256 |
| B | GLY257 |
| B | HOH388 |
| B | HOH403 |
| B | HOH407 |
| B | HOH555 |
| site_id | AC3 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD C 379 |
| Chain | Residue |
| C | ASN91 |
| C | VAL95 |
| C | GLY123 |
| C | VAL124 |
| C | GLY125 |
| C | ASN126 |
| C | VAL127 |
| C | ASP146 |
| C | PRO147 |
| C | PRO148 |
| C | HIS174 |
| C | THR175 |
| C | PRO176 |
| C | TYR178 |
| C | TYR183 |
| C | THR185 |
| C | ALA206 |
| C | CYS207 |
| C | ARG208 |
| C | ASP232 |
| C | HIS254 |
| C | ALA256 |
| C | GLY257 |
| C | HOH380 |
| C | HOH393 |
| C | HOH402 |
| C | HOH423 |
| site_id | AC4 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD D 379 |
| Chain | Residue |
| D | HIS254 |
| D | ALA256 |
| D | GLY257 |
| D | HOH398 |
| D | HOH413 |
| D | HOH414 |
| D | HOH519 |
| D | ASN91 |
| D | VAL95 |
| D | GLY123 |
| D | GLY125 |
| D | ASN126 |
| D | VAL127 |
| D | CYS145 |
| D | ASP146 |
| D | PRO147 |
| D | PRO148 |
| D | HIS174 |
| D | THR175 |
| D | PRO176 |
| D | TYR178 |
| D | TYR183 |
| D | THR185 |
| D | ALA206 |
| D | CYS207 |
| D | ARG208 |
| D | ASP232 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAD E 379 |
| Chain | Residue |
| E | ASN91 |
| E | VAL95 |
| E | GLY123 |
| E | GLY125 |
| E | ASN126 |
| E | VAL127 |
| E | ASP146 |
| E | PRO147 |
| E | PRO148 |
| E | ARG149 |
| E | HIS174 |
| E | THR175 |
| E | PRO176 |
| E | TYR178 |
| E | TYR183 |
| E | THR185 |
| E | ALA206 |
| E | CYS207 |
| E | ARG208 |
| E | ASP232 |
| E | HIS254 |
| E | ALA256 |
| E | GLY257 |
| E | HOH393 |
| E | HOH440 |
| site_id | AC6 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAD F 379 |
| Chain | Residue |
| F | ASN91 |
| F | VAL95 |
| F | GLY123 |
| F | VAL124 |
| F | GLY125 |
| F | ASN126 |
| F | VAL127 |
| F | CYS145 |
| F | ASP146 |
| F | PRO147 |
| F | PRO148 |
| F | HIS174 |
| F | THR175 |
| F | PRO176 |
| F | TYR178 |
| F | TYR183 |
| F | THR185 |
| F | ALA206 |
| F | CYS207 |
| F | ASP232 |
| F | HIS254 |
| F | GLY257 |
| F | HOH383 |
| F | HOH404 |
| F | HOH412 |
| site_id | AC7 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD G 379 |
| Chain | Residue |
| G | ASN91 |
| G | VAL95 |
| G | GLY123 |
| G | VAL124 |
| G | GLY125 |
| G | ASN126 |
| G | VAL127 |
| G | CYS145 |
| G | ASP146 |
| G | PRO147 |
| G | PRO148 |
| G | HIS174 |
| G | THR175 |
| G | PRO176 |
| G | TYR183 |
| G | THR185 |
| G | ALA206 |
| G | CYS207 |
| G | ARG208 |
| G | ASP232 |
| G | HIS254 |
| G | ALA256 |
| G | GLY257 |
| G | HOH386 |
| G | HOH393 |
| G | HOH399 |
| site_id | AC8 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAD H 379 |
| Chain | Residue |
| H | ASN91 |
| H | VAL95 |
| H | VAL122 |
| H | GLY123 |
| H | GLY125 |
| H | ASN126 |
| H | VAL127 |
| H | CYS145 |
| H | ASP146 |
| H | PRO147 |
| H | PRO148 |
| H | HIS174 |
| H | THR175 |
| H | PRO176 |
| H | TYR183 |
| H | THR185 |
| H | ALA206 |
| H | CYS207 |
| H | ARG208 |
| H | ASP232 |
| H | VAL233 |
| H | HIS254 |
| H | ALA256 |
| H | GLY257 |
| H | HOH383 |
Functional Information from PROSITE/UniProt
| site_id | PS00065 |
| Number of Residues | 28 |
| Details | D_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. IGIVGvGNVGsrlqtrlealgir.TLlCD |
| Chain | Residue | Details |
| A | ILE119-ASP146 |
| site_id | PS00671 |
| Number of Residues | 17 |
| Details | D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. LKpGaILINaCRGpVVD |
| Chain | Residue | Details |
| A | LEU197-ASP213 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01825 |
| Chain | Residue | Details |
| A | ARG208 | |
| E | GLU237 | |
| F | ARG208 | |
| F | GLU237 | |
| G | ARG208 | |
| G | GLU237 | |
| H | ARG208 | |
| H | GLU237 | |
| A | GLU237 | |
| B | ARG208 | |
| B | GLU237 | |
| C | ARG208 | |
| C | GLU237 | |
| D | ARG208 | |
| D | GLU237 | |
| E | ARG208 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01825 |
| Chain | Residue | Details |
| A | HIS254 | |
| B | HIS254 | |
| C | HIS254 | |
| D | HIS254 | |
| E | HIS254 | |
| F | HIS254 | |
| G | HIS254 | |
| H | HIS254 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 56 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01825 |
| Chain | Residue | Details |
| A | SER45 | |
| B | ASP146 | |
| B | THR175 | |
| B | ASP232 | |
| B | GLY257 | |
| B | TYR258 | |
| C | SER45 | |
| C | THR66 | |
| C | ASP146 | |
| C | THR175 | |
| C | ASP232 | |
| A | THR66 | |
| C | GLY257 | |
| C | TYR258 | |
| D | SER45 | |
| D | THR66 | |
| D | ASP146 | |
| D | THR175 | |
| D | ASP232 | |
| D | GLY257 | |
| D | TYR258 | |
| E | SER45 | |
| A | ASP146 | |
| E | THR66 | |
| E | ASP146 | |
| E | THR175 | |
| E | ASP232 | |
| E | GLY257 | |
| E | TYR258 | |
| F | SER45 | |
| F | THR66 | |
| F | ASP146 | |
| F | THR175 | |
| A | THR175 | |
| F | ASP232 | |
| F | GLY257 | |
| F | TYR258 | |
| G | SER45 | |
| G | THR66 | |
| G | ASP146 | |
| G | THR175 | |
| G | ASP232 | |
| G | GLY257 | |
| G | TYR258 | |
| A | ASP232 | |
| H | SER45 | |
| H | THR66 | |
| H | ASP146 | |
| H | THR175 | |
| H | ASP232 | |
| H | GLY257 | |
| H | TYR258 | |
| A | GLY257 | |
| A | TYR258 | |
| B | SER45 | |
| B | THR66 |
