Table 2. Common Structural Elements in Horse and Yeast ADHs Interrupted by Insertions or Deletions^a.

similarities		differences
horse	yeast	horse	yeast	location of change
		1–6	1–3	amino terminal
7–57	4–54	58	55–57	substrate binding site
59–94	58–93	95	94, 95	start of structural Zn loop
96–113	96–113	114–143	114–122	excursionary loop
144–183	123–162	184, 185	163	connect αA, βA
186–199	164–177	200	178, 179	connect βA, αB
201–216	180–195	217, 218	196	connect αB, βB
219–247	197–225	248, 249	226	connect βC, αCD
250–283	227–260	284, 285	261	connect αE, βE
286–296	262–272	297, 298	273	connect βE, βS
299–309	274–284	310	285, 286	connect βS, βF
311–319	287–295	320–323	296	connect βF, α3
324–339	297–312	340–347	313–317	connect α3, βI:5
348–366	318–336	367	337–338	connect α4, βI:6
368–374	339–345		346, 347	carboxyl terminal

^aThe structures of the ternary complexes of yeast (PDB entry 4W6Z) and horse liver (PDB entry 4DXH) with NAD and 2,2,2-trifluoroethanol, A chains, were superimposed with O, using 16 common structural elements with 248 residues (Table 4S of the Supporting Information). Inspection of the structures identified the similar structural elements (helices, β-strands, and loops), as described previously,² and the sites of insertions and deletions. Differences of ∼3 Å in Cα positions were tolerated, as there are shifts in the structural elements, with retention of the conformation. PDBeFold on the EMBL-EBI server aligned 319 residues in 21 structural elements with an rmsd of 2.3 Å, but the structure differed at 11 positions because of shifts of a residue in the alignment.