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5NNO

Structure of TbALDH3 complexed with NAD and AN3057 aldehyde

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
A0005737cellular_componentcytoplasm
A0006081biological_processaldehyde metabolic process
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0000166molecular_functionnucleotide binding
B0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
B0005737cellular_componentcytoplasm
B0006081biological_processaldehyde metabolic process
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Functional Information from PDB Data
site_idAC1
Number of Residues22
Detailsbinding site for residue NAD A 601
ChainResidue
AILE124
ATYR199
ATHR200
AGLY201
ASER202
AVAL205
AGLU223
ALEU224
AGLY225
ASER259
AGLU365
AGLY125
ALEU393
APHE433
A92N602
ATRP127
AASN128
ALEU133
ALYS151
AGLU154
AVAL183
ATHR186

site_idAC2
Number of Residues11
Detailsbinding site for residue 92N A 602
ChainResidue
AMET75
APRO79
AASN128
ATYR129
ALEU132
ATRP249
ATHR258
ASER259
AALA426
AGLY427
ANAD601

site_idAC3
Number of Residues27
Detailsbinding site for residue NAD B 601
ChainResidue
BILE124
BGLY125
BTHR126
BTRP127
BASN128
BLEU133
BLYS151
BSER153
BGLU154
BTHR186
BTYR199
BTHR200
BGLY201
BSER202
BVAL205
BGLU223
BLEU224
BGLY225
BSER259
BGLU365
BLEU393
BPHE433
B92N602
BHOH716
BHOH719
BHOH767
BHOH769

site_idAC4
Number of Residues9
Detailsbinding site for residue 92N B 602
ChainResidue
BMET75
BPRO79
BASN128
BTYR129
BLEU132
BTHR258
BSER259
BGLY427
BNAD601

Functional Information from PROSITE/UniProt
site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP
ChainResidueDetails
ALEU222-PRO229

247947

PDB entries from 2026-01-21

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