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
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
A | 0008957 | molecular_function | phenylacetaldehyde dehydrogenase activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
A | 0043878 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
B | 0008957 | molecular_function | phenylacetaldehyde dehydrogenase activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
B | 0043878 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue PEG A 601 |
Chain | Residue |
A | LYS216 |
A | GLN242 |
A | TRP246 |
B | ARG32 |
B | GLU38 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue PEG A 602 |
Chain | Residue |
A | GLN348 |
A | TYR351 |
B | LYS216 |
B | GLY217 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue PEG A 603 |
Chain | Residue |
A | ARG452 |
A | SO4605 |
B | PHE63 |
B | LEU149 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue PPI A 604 |
Chain | Residue |
A | GLU113 |
A | ARG294 |
A | THR296 |
A | VAL463 |
A | GLY464 |
A | ALA465 |
A | PHE471 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 605 |
Chain | Residue |
A | ARG452 |
A | LYS475 |
A | PEG603 |
A | HOH767 |
B | GLN233 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 606 |
Chain | Residue |
A | GLN233 |
A | HOH754 |
B | ARG452 |
B | LYS475 |
site_id | AC7 |
Number of Residues | 1 |
Details | binding site for residue SO4 A 607 |
Chain | Residue |
A | ARG53 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 608 |
Chain | Residue |
A | ARG272 |
A | GLY417 |
A | ILE418 |
A | TRP443 |
A | HOH776 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue PEG B 701 |
Chain | Residue |
A | ARG60 |
A | PHE63 |
A | LEU149 |
B | ARG452 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue PEG B 702 |
Chain | Residue |
A | ILE486 |
A | GLU490 |
B | GLN131 |
B | ILE486 |
site_id | AD2 |
Number of Residues | 7 |
Details | binding site for residue MPO B 703 |
Chain | Residue |
A | ARG346 |
A | HIS350 |
A | ARG399 |
A | VAL405 |
B | ARG37 |
B | GLU341 |
B | SO4706 |
site_id | AD3 |
Number of Residues | 2 |
Details | binding site for residue GOL B 704 |
Chain | Residue |
B | HIS440 |
B | HIS442 |
site_id | AD4 |
Number of Residues | 7 |
Details | binding site for residue PPI B 705 |
Chain | Residue |
B | ARG294 |
B | THR296 |
B | THR462 |
B | VAL463 |
B | GLY464 |
B | ALA465 |
B | PHE471 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue SO4 B 706 |
Chain | Residue |
A | ARG399 |
B | ARG37 |
B | ARG367 |
B | MPO703 |
B | HOH828 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue SO4 B 707 |
Chain | Residue |
B | SER240 |
B | ARG342 |
B | ARG346 |
B | HOH812 |
B | HOH877 |
site_id | AD7 |
Number of Residues | 8 |
Details | binding site for residue SO4 B 708 |
Chain | Residue |
A | ARG352 |
B | LYS182 |
B | SER184 |
B | GLU185 |
B | GLY213 |
B | ARG342 |
B | HOH801 |
B | HOH829 |
Functional Information from PROSITE/UniProt