Literature summary extracted from
Seo, K.H.; Zhuang, N.; Chen, C.; Song, J.Y.; Kang, H.L.; Rhee, K.H.; Lee, K.H.
Unusual NADPH conformation in the crystal structure of a cinnamyl alcohol dehydrogenase from Helicobacter pylori in complex with NADP(H) and substrate docking analysis (2012), FEBS Lett., 586, 337-343.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
1.1.1.195 |
- |
Helicobacter pylori |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
1.1.1.195 |
in complex with NADP(H), to 2.18 A resolution. NADP(H) is bound through hydrophobic interactions within the well-conserved GXGGXG motif from residues Gly184 to Gly189 and the adenine ring is the syn-conformation and is sandwiched between the guanidino group of Arg208 and Thr244 side chains. The aromatic side chains of residues Phe114 and Tyr116 in the active site could bind aromatic aldehydes by stacking the aromatic head of the substrates |
Helicobacter pylori |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.1.1.195 |
Helicobacter pylori |
D0ITF8 |
putative |
- |