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2YQ5

Crystal Structure of D-isomer specific 2-hydroxyacid dehydrogenase from Lactobacillus delbrueckii ssp. bulgaricus: NAD complexed form

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0008720molecular_functionD-lactate dehydrogenase activity
A0016491molecular_functionoxidoreductase activity
A0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0051287molecular_functionNAD binding
B0000166molecular_functionnucleotide binding
B0008720molecular_functionD-lactate dehydrogenase activity
B0016491molecular_functionoxidoreductase activity
B0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0051287molecular_functionNAD binding
C0000166molecular_functionnucleotide binding
C0008720molecular_functionD-lactate dehydrogenase activity
C0016491molecular_functionoxidoreductase activity
C0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0051287molecular_functionNAD binding
D0000166molecular_functionnucleotide binding
D0008720molecular_functionD-lactate dehydrogenase activity
D0016491molecular_functionoxidoreductase activity
D0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE NAD A 0
ChainResidue
AILE107
AHIS207
ATHR208
APRO209
ACYS235
AALA236
AARG237
AASP261
AHIS298
AALA300
APHE301
AVAL156
AGLY157
AHIS158
AILE159
ATYR177
AASP178
AVAL179
AALA180

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE NAD B 0
ChainResidue
BTYR102
BILE107
BGLY155
BVAL156
BGLY157
BHIS158
BILE159
BTYR177
BASP178
BVAL179
BALA180
BHIS207
BTHR208
BPRO209
BCYS235
BALA236
BARG237
BASP261
BHIS298
BALA300
BPHE301

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE NAD C 0
ChainResidue
CTYR102
CILE107
CGLY155
CVAL156
CGLY157
CHIS158
CILE159
CTYR177
CASP178
CVAL179
CALA180
CHIS207
CTHR208
CPRO209
CCYS235
CALA236
CARG237
CASP261
CHIS298
CALA300
CPHE301
CHOH2001

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE NAD D 0
ChainResidue
DTYR102
DILE107
DGLY155
DVAL156
DGLY157
DHIS158
DILE159
DTYR177
DASP178
DALA180
DHIS207
DTHR208
DPRO209
DMET217
DCYS235
DARG237
DASP261
DHIS298
DALA300
DPHE301

Functional Information from PROSITE/UniProt
site_idPS00670
Number of Residues23
DetailsD_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. VLkeADIVsLHtPlfpsTenMiG
ChainResidueDetails
AVAL197-GLY219

site_idPS00671
Number of Residues17
DetailsD_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. MKkSaYLINcARGeLVD
ChainResidueDetails
AMET226-ASP242

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PDB entries from 2024-07-10

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