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6ABI

The apo-structure of D-lactate dehydrogenase from Fusobacterium nucleatum

Replaces:  3WWY
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
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue SO4 A 401
ChainResidue
AVAL35
AARG36
AHOH503
AHOH545
BLYS34
BVAL35

site_idAC2
Number of Residues5
Detailsbinding site for residue SO4 A 402
ChainResidue
AHOH507
BLYS95
APRO209
ALEU210
AARG237

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 A 403
ChainResidue
ATHR313
AASN316
AHOH561

site_idAC4
Number of Residues3
Detailsbinding site for residue SO4 A 404
ChainResidue
AHIS105
ALYS156
BTYR145

site_idAC5
Number of Residues5
Detailsbinding site for residue GOL A 405
ChainResidue
AASN119
ALYS121
AGLY229
AGLY256
AHOH532

site_idAC6
Number of Residues5
Detailsbinding site for residue SO4 B 401
ChainResidue
ATYR145
BHIS105
BLYS156
BGOL409
BHOH511

site_idAC7
Number of Residues7
Detailsbinding site for residue SO4 B 402
ChainResidue
BCYS79
BALA80
BARG98
BPRO100
BALA101
BARG237
BGOL408

site_idAC8
Number of Residues5
Detailsbinding site for residue SO4 B 403
ChainResidue
ALYS95
BPRO209
BLEU210
BARG237
BGOL410

site_idAC9
Number of Residues3
Detailsbinding site for residue SO4 B 404
ChainResidue
BTHR313
BASN316
BHOH521

site_idAD1
Number of Residues8
Detailsbinding site for residue GOL B 405
ChainResidue
AASP143
BPRO104
BHIS105
BALA106
BGLU305
BALA306
BHOH501
BHOH511

site_idAD2
Number of Residues9
Detailsbinding site for residue GOL B 406
ChainResidue
APHE321
BGLY155
BASP176
BLEU177
BPHE178
BGOL410
BHOH502
BHOH508
BHOH557

site_idAD3
Number of Residues5
Detailsbinding site for residue GOL B 407
ChainResidue
BASN119
BLYS121
BGLY229
BGLY256
BHOH541

site_idAD4
Number of Residues6
Detailsbinding site for residue GOL B 408
ChainResidue
BILE107
BTHR235
BGLY236
BARG237
BHIS298
BSO4402

site_idAD5
Number of Residues5
Detailsbinding site for residue GOL B 409
ChainResidue
AARG325
BTYR102
BLYS156
BSO4401
BHOH511

site_idAD6
Number of Residues8
Detailsbinding site for residue GOL B 410
ChainResidue
AASP320
APHE321
AGLY324
AARG325
ALEU327
BPRO209
BSO4403
BGOL406

site_idAD7
Number of Residues6
Detailsbinding site for residue GOL B 411
ChainResidue
BVAL99
BPRO100
BTYR102
BALA309
BILE310
BTHR313

Functional Information from PROSITE/UniProt
site_idPS00065
Number of Residues28
DetailsD_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. AGIIGtGKIGqilikilrgfdmk.VIaYD
ChainResidueDetails
AALA149-ASP176

site_idPS00670
Number of Residues23
DetailsD_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. LYanSDIIsLNcPltkdTkyMiN
ChainResidueDetails
ALEU197-ASN219

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

221051

PDB entries from 2024-06-12

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