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2DLD

D-LACTATE DEHYDROGENASE COMPLEXED WITH NADH AND OXAMATE

Functional Information from GO Data
ChainGOidnamespacecontents
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
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
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE NAI A 401
ChainResidue
ATHR154
AASN213
ACYS234
ASER235
AARG236
ATHR261
AHIS297
AALA299
APHE337
AOXM402
AGLY155
AHIS156
AILE157
AASP176
AILE177
AHIS206
AVAL207
APRO208

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE OXM A 402
ChainResidue
ASER235
AARG236
AHIS297
ANAI401

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE NAI B 401
ChainResidue
BTHR154
BGLY155
BHIS156
BILE157
BASP176
BILE177
BHIS206
BVAL207
BPRO208
BASN213
BCYS234
BSER235
BARG236
BASP260
BTHR261
BHIS297
BALA299
BOXM402

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE OXM B 402
ChainResidue
BARG236
BHIS297
BNAI401

Functional Information from PROSITE/UniProt
site_idPS00065
Number of Residues28
DetailsD_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. VGVVGtGHIGqvfmrimegfgak.VIaYD
ChainResidueDetails
AVAL149-ASP176

site_idPS00670
Number of Residues23
DetailsD_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. LYkqADVIsLHvPdvpaNvhMiN
ChainResidueDetails
ALEU196-ASN218

site_idPS00671
Number of Residues17
DetailsD_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. MKdGvVIVNcSRGrLVD
ChainResidueDetails
AMET225-ASP241

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P26297
ChainResidueDetails
AGLY237
AVAL266
BGLY237
BVAL266

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P26297
ChainResidueDetails
ATHR298
BTHR298

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|Ref.3
ChainResidueDetails
AILE157
ASER235
BILE157
BSER235

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|Ref.3
ChainResidueDetails
AILE177
APRO208
AVAL214
ATHR261
BILE177
BPRO208
BVAL214
BTHR261

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1j49
ChainResidueDetails
AARG236
AASP209
AGLU265
AHIS297
AASP260

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1j49
ChainResidueDetails
BARG236
BASP209
BGLU265
BHIS297
BASP260

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1j49
ChainResidueDetails
AGLU265
AHIS297

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1j49
ChainResidueDetails
BGLU265
BHIS297

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PDB entries from 2024-07-10

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