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6FKU

Structure and function of aldehyde dehydrogenase from Thermus thermophilus: An enzyme with an evolutionarily-distinct C-terminal arm (Recombinant protein with shortened C-terminal, in complex with NADP)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
A0008957molecular_functionphenylacetaldehyde dehydrogenase activity
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0043878molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity
B0000166molecular_functionnucleotide binding
B0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
B0008957molecular_functionphenylacetaldehyde dehydrogenase activity
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0043878molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue PGE A 701
ChainResidue
AALA305
AGLU309
ALYS414
AHOH817

site_idAC2
Number of Residues3
Detailsbinding site for residue PEG A 702
ChainResidue
AARG346
AARG399
AGLU403

site_idAC3
Number of Residues4
Detailsbinding site for residue PGE A 703
ChainResidue
BGLN242
BNAP605
AGLU38
BLYS216

site_idAC4
Number of Residues5
Detailsbinding site for residue PGE A 704
ChainResidue
ALEU12
AGLU88
ATHR91
APHE192
AVAL193

site_idAC5
Number of Residues3
Detailsbinding site for residue PGE A 705
ChainResidue
ALYS216
AGLN221
ANAP708

site_idAC6
Number of Residues6
Detailsbinding site for residue PG4 A 706
ChainResidue
ALEU149
APHE232
AGLN233
APGE707
BLYS475
BHOH739

site_idAC7
Number of Residues7
Detailsbinding site for residue PGE A 707
ChainResidue
APHE63
APRO148
ALEU149
AGLN233
ATYR494
APG4706
BARG452

site_idAC8
Number of Residues31
Detailsbinding site for residue NAP A 708
ChainResidue
AILE155
ATHR156
AALA157
AASN159
ALYS182
ASER184
AGLU185
AGLY213
AGLY214
AGLY215
ALYS216
AGLY220
AGLN221
APHE237
ATHR238
AGLY239
ASER240
AVAL243
ATRP246
AGLU261
ALEU262
AGLY263
ACYS295
AARG342
APHE343
AGLU404
APHE406
APHE471
APGE705
AHOH803
AHOH808

site_idAC9
Number of Residues6
Detailsbinding site for residue 1PE A 709
ChainResidue
AGLN131
AILE486
AGLU490
BGLN131
BILE486
BGLU490

site_idAD1
Number of Residues3
Detailsbinding site for residue SO4 A 710
ChainResidue
AARG37
AARG367
BARG399

site_idAD2
Number of Residues7
Detailsbinding site for residue SO4 A 711
ChainResidue
AARG294
ATHR296
AVAL463
AGLY464
AALA465
APHE471
AHOH814

site_idAD3
Number of Residues4
Detailsbinding site for residue PEG B 601
ChainResidue
ALYS216
BGLN348
BTYR351
BARG365

site_idAD4
Number of Residues8
Detailsbinding site for residue 1PE B 602
ChainResidue
AARG452
ALYS475
AGLY478
BLEU149
BGLN233
BASN254
BLEU255
BPGE603

site_idAD5
Number of Residues6
Detailsbinding site for residue PGE B 603
ChainResidue
AARG452
BARG60
BALA64
BARG68
BLEU149
B1PE602

site_idAD6
Number of Residues3
Detailsbinding site for residue 1PE B 604
ChainResidue
BLYS414
BALA305
BGLU309

site_idAD7
Number of Residues30
Detailsbinding site for residue NAP B 605
ChainResidue
APGE703
BILE155
BTHR156
BALA157
BASN159
BLYS182
BSER184
BGLU185
BGLY213
BGLY215
BLYS216
BGLY220
BGLN221
BPHE237
BTHR238
BGLY239
BSER240
BVAL243
BTRP246
BGLU261
BLEU262
BGLY263
BCYS295
BARG342
BPHE343
BGLU404
BPHE406
BPHE471
BHOH761
BHOH764

site_idAD8
Number of Residues2
Detailsbinding site for residue PEG B 606
ChainResidue
BGLU88
BTHR91

site_idAD9
Number of Residues7
Detailsbinding site for residue SO4 B 607
ChainResidue
BARG294
BTHR296
BVAL463
BGLY464
BALA465
BPHE471
BHOH728

Functional Information from PROSITE/UniProt
site_idPS00213
Number of Residues13
DetailsLIPOCALIN Lipocalin signature. DLDl.AVEGAWWSA
ChainResidueDetails
AASP275-ALA287

site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKNP
ChainResidueDetails
ALEU260-PRO267

221051

PDB entries from 2024-06-12

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