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6FJX

Structure and function of aldehyde dehydrogenase from Thermus thermophilus: An enzyme with an evolutionarily-distinct C-terminal arm (Native protein)

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 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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