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6FK3

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

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 Residues5
Detailsbinding site for residue PEG A 601
ChainResidue
ALYS216
AGLN242
ATRP246
BARG32
BGLU38

site_idAC2
Number of Residues4
Detailsbinding site for residue PEG A 602
ChainResidue
AGLN348
ATYR351
BLYS216
BGLY217

site_idAC3
Number of Residues4
Detailsbinding site for residue PEG A 603
ChainResidue
AARG452
ASO4605
BPHE63
BLEU149

site_idAC4
Number of Residues7
Detailsbinding site for residue PPI A 604
ChainResidue
AGLU113
AARG294
ATHR296
AVAL463
AGLY464
AALA465
APHE471

site_idAC5
Number of Residues5
Detailsbinding site for residue SO4 A 605
ChainResidue
AARG452
ALYS475
APEG603
AHOH767
BGLN233

site_idAC6
Number of Residues4
Detailsbinding site for residue SO4 A 606
ChainResidue
AGLN233
AHOH754
BARG452
BLYS475

site_idAC7
Number of Residues1
Detailsbinding site for residue SO4 A 607
ChainResidue
AARG53

site_idAC8
Number of Residues5
Detailsbinding site for residue SO4 A 608
ChainResidue
AARG272
AGLY417
AILE418
ATRP443
AHOH776

site_idAC9
Number of Residues4
Detailsbinding site for residue PEG B 701
ChainResidue
AARG60
APHE63
ALEU149
BARG452

site_idAD1
Number of Residues4
Detailsbinding site for residue PEG B 702
ChainResidue
AILE486
AGLU490
BGLN131
BILE486

site_idAD2
Number of Residues7
Detailsbinding site for residue MPO B 703
ChainResidue
AARG346
AHIS350
AARG399
AVAL405
BARG37
BGLU341
BSO4706

site_idAD3
Number of Residues2
Detailsbinding site for residue GOL B 704
ChainResidue
BHIS440
BHIS442

site_idAD4
Number of Residues7
Detailsbinding site for residue PPI B 705
ChainResidue
BARG294
BTHR296
BTHR462
BVAL463
BGLY464
BALA465
BPHE471

site_idAD5
Number of Residues5
Detailsbinding site for residue SO4 B 706
ChainResidue
AARG399
BARG37
BARG367
BMPO703
BHOH828

site_idAD6
Number of Residues5
Detailsbinding site for residue SO4 B 707
ChainResidue
BSER240
BARG342
BARG346
BHOH812
BHOH877

site_idAD7
Number of Residues8
Detailsbinding site for residue SO4 B 708
ChainResidue
AARG352
BLYS182
BSER184
BGLU185
BGLY213
BARG342
BHOH801
BHOH829

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

219140

PDB entries from 2024-05-01

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