1GDH
CRYSTAL STRUCTURE OF A NAD-DEPENDENT D-GLYCERATE DEHYDROGENASE AT 2.4 ANGSTROMS RESOLUTION
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 | 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 | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 322 |
| Chain | Residue |
| A | GLY100 |
| A | VAL101 |
| A | THR102 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 322 |
| Chain | Residue |
| B | HIS99 |
| B | GLY100 |
| B | VAL101 |
| B | THR102 |
| B | HOH354 |
| B | HOH376 |
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. LGIYGfGSIGqalakraqgfdmd.IDyFD |
| Chain | Residue | Details |
| A | LEU150-ASP177 |
| site_id | PS00670 |
| Number of Residues | 23 |
| Details | D_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. LLsvSQFFsLNaPstpeTryFfN |
| Chain | Residue | Details |
| A | LEU200-ASN222 |
| site_id | PS00671 |
| Number of Residues | 17 |
| Details | D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. LPqGaIVVNtARGdLVD |
| Chain | Residue | Details |
| A | LEU229-ASP245 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: |
| Chain | Residue | Details |
| A | GLY241 | |
| A | PRO270 | |
| B | GLY241 | |
| B | PRO270 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | ILE288 | |
| B | ILE288 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ILE158 | |
| B | ILE288 | |
| A | THR178 | |
| A | ALA239 | |
| A | VAL265 | |
| A | ILE288 | |
| B | ILE158 | |
| B | THR178 | |
| B | ALA239 | |
| B | VAL265 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 8120891 |
| Chain | Residue | Details |
| A | HIS287 | |
| A | GLU269 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 571 |
| Chain | Residue | Details |
| A | ARG240 | electrostatic stabiliser |
| A | GLU269 | electrostatic stabiliser |
| A | HIS287 | proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 571 |
| Chain | Residue | Details |
| B | ARG240 | electrostatic stabiliser |
| B | GLU269 | electrostatic stabiliser |
| B | HIS287 | proton acceptor, proton donor |
