4E5P
Thermostable phosphite dehydrogenase A176R variant in complex with NAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0050609 | molecular_function | phosphonate dehydrogenase activity |
| A | 0051287 | molecular_function | NAD binding |
| 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 | 0050609 | molecular_function | phosphonate dehydrogenase activity |
| B | 0051287 | molecular_function | NAD binding |
| 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 | 0050609 | molecular_function | phosphonate dehydrogenase activity |
| C | 0051287 | molecular_function | NAD binding |
| 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 | 0050609 | molecular_function | phosphonate dehydrogenase activity |
| D | 0051287 | molecular_function | NAD binding |
| 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 | 0050609 | molecular_function | phosphonate dehydrogenase activity |
| E | 0051287 | molecular_function | NAD binding |
| 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 | 0050609 | molecular_function | phosphonate dehydrogenase activity |
| F | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD A 800 |
| Chain | Residue |
| A | LYS76 |
| A | LEU208 |
| A | PRO209 |
| A | THR214 |
| A | PRO235 |
| A | CYS236 |
| A | ARG237 |
| A | ASP261 |
| A | HIS292 |
| A | GLY294 |
| A | HOH906 |
| A | THR104 |
| A | HOH910 |
| A | HOH931 |
| A | HOH939 |
| A | HOH959 |
| A | HOH979 |
| A | HOH1070 |
| A | HOH1117 |
| A | MET153 |
| A | GLY154 |
| A | ALA155 |
| A | ILE156 |
| A | ALA175 |
| A | ARG176 |
| A | ALA207 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAD B 800 |
| Chain | Residue |
| B | LYS76 |
| B | THR104 |
| B | GLY154 |
| B | ALA155 |
| B | ILE156 |
| B | ALA175 |
| B | ARG176 |
| B | LEU208 |
| B | PRO209 |
| B | THR214 |
| B | PRO235 |
| B | CYS236 |
| B | ARG237 |
| B | ASP261 |
| B | HIS292 |
| B | GLY294 |
| B | HOH912 |
| B | HOH919 |
| B | HOH926 |
| B | HOH964 |
| B | HOH983 |
| B | HOH990 |
| B | HOH1118 |
| site_id | AC3 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD C 800 |
| Chain | Residue |
| C | THR104 |
| C | GLY152 |
| C | MET153 |
| C | GLY154 |
| C | ALA155 |
| C | ILE156 |
| C | ALA175 |
| C | ARG176 |
| C | LYS177 |
| C | ALA207 |
| C | LEU208 |
| C | PRO209 |
| C | THR214 |
| C | LEU217 |
| C | PRO235 |
| C | CYS236 |
| C | ARG237 |
| C | ASP261 |
| C | HIS292 |
| C | GLY294 |
| C | HOH919 |
| C | HOH944 |
| C | HOH950 |
| C | HOH961 |
| C | HOH973 |
| C | HOH997 |
| C | HOH1036 |
| C | HOH1060 |
| site_id | AC4 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD D 800 |
| Chain | Residue |
| D | HOH951 |
| D | HOH959 |
| D | HOH1025 |
| D | HOH1039 |
| D | HOH1046 |
| D | HOH1085 |
| D | THR104 |
| D | GLY152 |
| D | MET153 |
| D | GLY154 |
| D | ALA155 |
| D | ILE156 |
| D | ALA175 |
| D | ARG176 |
| D | LYS177 |
| D | ALA207 |
| D | LEU208 |
| D | PRO209 |
| D | THR214 |
| D | PRO235 |
| D | CYS236 |
| D | ARG237 |
| D | ASP261 |
| D | HIS292 |
| D | GLY294 |
| D | HOH902 |
| D | HOH926 |
| D | HOH946 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE NAD E 800 |
| Chain | Residue |
| E | LYS76 |
| E | THR104 |
| E | GLY154 |
| E | ALA155 |
| E | ILE156 |
| E | ARG176 |
| E | LEU208 |
| E | PRO209 |
| E | THR214 |
| E | PRO235 |
| E | CYS236 |
| E | ARG237 |
| E | ASP261 |
| E | HIS292 |
| E | GLY294 |
| E | HOH917 |
| E | HOH928 |
| E | HOH943 |
| E | HOH954 |
| E | HOH965 |
| site_id | AC6 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD F 800 |
| Chain | Residue |
| F | THR104 |
| F | GLY152 |
| F | MET153 |
| F | GLY154 |
| F | ALA155 |
| F | ILE156 |
| F | ALA175 |
| F | ARG176 |
| F | LYS177 |
| F | ALA207 |
| F | LEU208 |
| F | PRO209 |
| F | THR214 |
| F | PRO235 |
| F | CYS236 |
| F | ARG237 |
| F | ASP261 |
| F | HIS292 |
| F | GLY294 |
| F | HOH931 |
| F | HOH951 |
| F | HOH957 |
| F | HOH987 |
| F | HOH990 |
| F | HOH1005 |
| F | HOH1043 |
| F | HOH1060 |
| F | HOH1072 |
Functional Information from PROSITE/UniProt
| site_id | PS00671 |
| Number of Residues | 17 |
| Details | D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. VRpGaLLVNpCRGsVVD |
| Chain | Residue | Details |
| A | VAL226-ASP242 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250 |
| Chain | Residue | Details |
| A | ARG237 | |
| E | GLU266 | |
| F | ARG237 | |
| F | GLU266 | |
| A | GLU266 | |
| B | ARG237 | |
| B | GLU266 | |
| C | ARG237 | |
| C | GLU266 | |
| D | ARG237 | |
| D | GLU266 | |
| E | ARG237 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | ACT_SITE: Proton donor => ECO:0000250 |
| Chain | Residue | Details |
| A | HIS292 | |
| B | HIS292 | |
| C | HIS292 | |
| D | HIS292 | |
| E | HIS292 | |
| F | HIS292 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 30 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ALA155 | |
| B | HIS292 | |
| C | ALA155 | |
| C | ALA175 | |
| C | PRO235 | |
| C | ASP261 | |
| C | HIS292 | |
| D | ALA155 | |
| D | ALA175 | |
| D | PRO235 | |
| D | ASP261 | |
| A | ALA175 | |
| D | HIS292 | |
| E | ALA155 | |
| E | ALA175 | |
| E | PRO235 | |
| E | ASP261 | |
| E | HIS292 | |
| F | ALA155 | |
| F | ALA175 | |
| F | PRO235 | |
| F | ASP261 | |
| A | PRO235 | |
| F | HIS292 | |
| A | ASP261 | |
| A | HIS292 | |
| B | ALA155 | |
| B | ALA175 | |
| B | PRO235 | |
| B | ASP261 |
