4ZGS
Identification of the pyruvate reductase of Chlamydomonas reinhardtii
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0008720 | molecular_function | D-lactate dehydrogenase (NAD+) 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 | 0051287 | molecular_function | NAD binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0008720 | molecular_function | D-lactate dehydrogenase (NAD+) 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 | 0051287 | molecular_function | NAD binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0008720 | molecular_function | D-lactate dehydrogenase (NAD+) activity |
| 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 | 0051287 | molecular_function | NAD binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0008720 | molecular_function | D-lactate dehydrogenase (NAD+) activity |
| 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 | 0051287 | molecular_function | NAD binding |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0008720 | molecular_function | D-lactate dehydrogenase (NAD+) activity |
| 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 | 0051287 | molecular_function | NAD binding |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0008720 | molecular_function | D-lactate dehydrogenase (NAD+) activity |
| 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 | 0051287 | molecular_function | NAD binding |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0008720 | molecular_function | D-lactate dehydrogenase (NAD+) activity |
| 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 | 0051287 | molecular_function | NAD binding |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0008720 | molecular_function | D-lactate dehydrogenase (NAD+) activity |
| 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 | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | binding site for residue NAD A 1000 |
| Chain | Residue |
| A | TYR134 |
| A | THR245 |
| A | VAL266 |
| A | SER267 |
| A | ARG268 |
| A | ASP292 |
| A | HIS335 |
| A | PHE338 |
| A | HOH1105 |
| A | GLY187 |
| A | ALA188 |
| A | ILE189 |
| A | ASP208 |
| A | CYS239 |
| A | PRO240 |
| A | LEU242 |
| A | SER244 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | binding site for residue NAD B 1000 |
| Chain | Residue |
| B | TYR134 |
| B | GLY187 |
| B | ALA188 |
| B | ILE189 |
| B | TYR207 |
| B | ASP208 |
| B | CYS239 |
| B | PRO240 |
| B | LEU242 |
| B | SER244 |
| B | THR245 |
| B | VAL266 |
| B | SER267 |
| B | ARG268 |
| B | ASP292 |
| B | HIS335 |
| B | ALA337 |
| B | PHE338 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | binding site for residue NAD C 1000 |
| Chain | Residue |
| C | TYR134 |
| C | GLY187 |
| C | ALA188 |
| C | ILE189 |
| C | TYR207 |
| C | ASP208 |
| C | ILE209 |
| C | PRO240 |
| C | LEU242 |
| C | SER244 |
| C | THR245 |
| C | VAL266 |
| C | SER267 |
| C | ARG268 |
| C | ASP292 |
| C | HIS335 |
| C | ALA337 |
| C | PHE338 |
| C | HOH1113 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | binding site for residue NAD D 1000 |
| Chain | Residue |
| D | TYR134 |
| D | GLY187 |
| D | ALA188 |
| D | ILE189 |
| D | TYR207 |
| D | ASP208 |
| D | CYS239 |
| D | PRO240 |
| D | SER244 |
| D | THR245 |
| D | VAL266 |
| D | SER267 |
| D | ARG268 |
| D | ASP292 |
| D | HIS335 |
| D | ALA337 |
| D | PHE338 |
| D | HOH1101 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | binding site for residue NAD E 1000 |
| Chain | Residue |
| E | TYR134 |
| E | GLY187 |
| E | ALA188 |
| E | ILE189 |
| E | TYR207 |
| E | ASP208 |
| E | CYS239 |
| E | PRO240 |
| E | LEU242 |
| E | SER244 |
| E | THR245 |
| E | VAL266 |
| E | SER267 |
| E | ARG268 |
| E | ASP292 |
| E | HIS335 |
| E | ALA337 |
| E | PHE338 |
| E | HOH1109 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | binding site for residue NAD F 1000 |
| Chain | Residue |
| F | SER244 |
| F | THR245 |
| F | VAL266 |
| F | SER267 |
| F | ARG268 |
| F | ASP292 |
| F | HIS335 |
| F | PHE338 |
| F | HOH1112 |
| F | TYR134 |
| F | GLY187 |
| F | ALA188 |
| F | ILE189 |
| F | ASP208 |
| F | ILE209 |
| F | CYS239 |
| F | PRO240 |
| site_id | AC7 |
| Number of Residues | 18 |
| Details | binding site for residue NAD G 1000 |
| Chain | Residue |
| G | TYR134 |
| G | GLY187 |
| G | ALA188 |
| G | ILE189 |
| G | TYR207 |
| G | ASP208 |
| G | ILE209 |
| G | PRO240 |
| G | SER244 |
| G | THR245 |
| G | VAL266 |
| G | SER267 |
| G | ARG268 |
| G | ASP292 |
| G | HIS335 |
| G | ALA337 |
| G | PHE338 |
| G | HOH1107 |
| site_id | AC8 |
| Number of Residues | 17 |
| Details | binding site for residue NAD H 1000 |
| Chain | Residue |
| H | TYR134 |
| H | GLY187 |
| H | ALA188 |
| H | ILE189 |
| H | TYR207 |
| H | ASP208 |
| H | CYS239 |
| H | PRO240 |
| H | SER244 |
| H | THR245 |
| H | VAL266 |
| H | SER267 |
| H | ARG268 |
| H | ASP292 |
| H | HIS335 |
| H | ALA337 |
| H | PHE338 |
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. VGVVGtGAIGqqaarilkgigck.VFaYD |
| Chain | Residue | Details |
| A | VAL181-ASP208 |
| site_id | PS00670 |
| Number of Residues | 23 |
| Details | D_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. LLamSDIVtLHcPllpsTrqLiN |
| Chain | Residue | Details |
| A | LEU228-ASN250 |
| site_id | PS00671 |
| Number of Residues | 17 |
| Details | D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. MKkGvMLINvSRGgLID |
| Chain | Residue | Details |
| A | MET257-ASP273 |
