1HET

atomic X-ray structure of liver alcohol dehydrogenase containing a hydroxide adduct to NADH

Summary for 1HET

• Entry DOI: 10.2210/pdb1het/pdb
• Related: 1A71 1A72 1AXE 1AXG 1BTO 1HEU 1LDE 1LDY 1QLH 1QLJ 3BTO
• Descriptor: ALCOHOL DEHYDROGENASE E CHAIN, ZINC ION, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (5 entities in total)
• Functional Keywords: oxidoreductase, oxidoreductase(nad(a)-choh(d))
• Biological source: EQUUS CABALLUS (DOMESTIC HORSE)
• Total number of polymer chains: 2
• Total formula weight: 81649.55

Authors

Meijers, R.,Morris, R.J.,Adolph, H.W.,Merli, A.,Lamzin, V.S.,Cedergen-Zeppezauer, E.S. (deposition date: 2000-11-25, release date: 2001-05-31, Last modification date: 2023-12-13)

Primary citation

Meijers, R.,Morris, R.J.,Adolph, H.W.,Merli, A.,Lamzin, V.S.,Cedergen-Zeppezauer, E.S.
On the Enzymatic Activation of Nadh
J.Biol.Chem., 276:9316-, 2001

PubMed Abstract: Atomic (1 A) resolution x-ray structures of horse liver alcohol dehydrogenase in complex with NADH revealed the formation of an adduct in the active site between a metal-bound water and NADH. Furthermore, a pronounced distortion of the pyridine ring of NADH was observed. A series of quantum chemical calculations on the water-nicotinamide adduct showed that the puckering of the pyridine ring in the crystal structures can only be reproduced when the water is considered a hydroxide ion. These observations provide fundamental insight into the enzymatic activation of NADH for hydride transfer.

PubMed: 11134046
DOI: 10.1074/JBC.M010870200

Experimental method

X-RAY DIFFRACTION (1.15 Å)