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1GDH

CRYSTAL STRUCTURE OF A NAD-DEPENDENT D-GLYCERATE DEHYDROGENASE AT 2.4 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0008465molecular_functionglycerate dehydrogenase activity
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0016618molecular_functionhydroxypyruvate reductase activity
A0030267molecular_functionglyoxylate reductase (NADPH) activity
A0051287molecular_functionNAD binding
B0005829cellular_componentcytosol
B0008465molecular_functionglycerate dehydrogenase activity
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0016618molecular_functionhydroxypyruvate reductase activity
B0030267molecular_functionglyoxylate reductase (NADPH) activity
B0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 322
ChainResidue
AGLY100
AVAL101
ATHR102

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 322
ChainResidue
BHIS99
BGLY100
BVAL101
BTHR102
BHOH354
BHOH376

Functional Information from PROSITE/UniProt
site_idPS00065
Number of Residues28
DetailsD_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. LGIYGfGSIGqalakraqgfdmd.IDyFD
ChainResidueDetails
ALEU150-ASP177

site_idPS00670
Number of Residues23
DetailsD_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. LLsvSQFFsLNaPstpeTryFfN
ChainResidueDetails
ALEU200-ASN222

site_idPS00671
Number of Residues17
DetailsD_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. LPqGaIVVNtARGdLVD
ChainResidueDetails
ALEU229-ASP245

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE:
ChainResidueDetails
AGLY241
APRO270
BGLY241
BPRO270

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor
ChainResidueDetails
AILE288
BILE288

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AILE158
BILE288
ATHR178
AALA239
AVAL265
AILE288
BILE158
BTHR178
BALA239
BVAL265

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 571
ChainResidueDetails
AGLY241electrostatic stabiliser
APRO270electrostatic stabiliser
AILE288proton acceptor, proton donor

site_idMCSA2
Number of Residues3
DetailsM-CSA 571
ChainResidueDetails
BGLY241electrostatic stabiliser
BPRO270electrostatic stabiliser
BILE288proton acceptor, proton donor

218853

PDB entries from 2024-04-24

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