4NU5
Crystal Structure of PTDH R301A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0008465 | molecular_function | hydroxypyruvate reductase (NADH) activity |
| 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 | 0016618 | molecular_function | hydroxypyruvate reductase [NAD(P)H] activity |
| A | 0030267 | molecular_function | glyoxylate reductase (NADPH) activity |
| A | 0050609 | molecular_function | phosphonate dehydrogenase activity |
| A | 0051287 | molecular_function | NAD binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0008465 | molecular_function | hydroxypyruvate reductase (NADH) activity |
| 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 | 0016618 | molecular_function | hydroxypyruvate reductase [NAD(P)H] activity |
| B | 0030267 | molecular_function | glyoxylate reductase (NADPH) activity |
| B | 0050609 | molecular_function | phosphonate dehydrogenase activity |
| B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD A 800 |
| Chain | Residue |
| A | LYS76 |
| A | ALA175 |
| A | ALA176 |
| A | LYS177 |
| A | ALA207 |
| A | LEU208 |
| A | PRO209 |
| A | THR214 |
| A | PRO235 |
| A | CYS236 |
| A | ARG237 |
| A | GLY77 |
| A | ASP261 |
| A | HIS292 |
| A | GLY294 |
| A | HOH914 |
| A | HOH922 |
| A | HOH974 |
| A | HOH989 |
| A | HOH1002 |
| A | HOH1050 |
| A | HOH1052 |
| A | LEU100 |
| A | THR104 |
| A | GLY152 |
| A | MET153 |
| A | GLY154 |
| A | ALA155 |
| A | ILE156 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD B 800 |
| Chain | Residue |
| B | LYS76 |
| B | GLY77 |
| B | THR104 |
| B | MET153 |
| B | GLY154 |
| B | ALA155 |
| B | ILE156 |
| B | ALA176 |
| B | LYS177 |
| B | ALA207 |
| B | LEU208 |
| B | PRO209 |
| B | THR214 |
| B | PRO235 |
| B | CYS236 |
| B | ARG237 |
| B | ASP261 |
| B | HIS292 |
| B | GLY294 |
| B | HOH916 |
| B | HOH919 |
| B | HOH943 |
| B | HOH1000 |
| B | HOH1008 |
| B | HOH1063 |
| B | HOH1075 |
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 | 4 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
