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 | glycerate dehydrogenase 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 activity |
A | 0030267 | molecular_function | glyoxylate reductase (NADPH) activity |
A | 0051287 | molecular_function | NAD binding |
B | 0005829 | cellular_component | cytosol |
B | 0008465 | molecular_function | glycerate dehydrogenase 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 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 | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 571 |
Chain | Residue | Details |
A | GLY241 | electrostatic stabiliser |
A | PRO270 | electrostatic stabiliser |
A | ILE288 | proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 571 |
Chain | Residue | Details |
B | GLY241 | electrostatic stabiliser |
B | PRO270 | electrostatic stabiliser |
B | ILE288 | proton acceptor, proton donor |