. 2009 Jun 3;9:39. doi: 10.1186/1472-6807-9-39

Table 5.

Docking of acetylcholine and butyrylcholine

	Docking into:
	X-ray structures		Substrate-imprinted structures

Structure	ACh	BuCh	ACh	BuCh
Torpedo californica acetylcholine esterase
Experimental data	+	-	+	-
1CFJ^a	+	+	+	-
1DX6^a	+	+	+	+
1E3Q^a	-	-	+	-
1EVE^a	+	+	+	-
1VXR^{a, b}	-	-	-	-
1QIM	+	+	+	-
No. false predictions	2	4	1	1

human butyrylcholine esterase
Experimental data	+	+	+	+
1P0M	-	-	-	-
1XLU^a	+	+	+	+
1XLV^a	+	+	+	+
1XLW^a	-	-	+	+
No. false predictions	2	2	1	1

Docking of ACh and BuCh into six X-ray structures of the acetylcholine esterase from Torpedo californica and four X-ray structures of the human butyrylcholine esterase using FlexX. The substrates were docked into the not optimised X-ray structures and the substrate-imprinted structures. "+" and "-" indicate that the docking results predict ACh or BuCh to be a substrate or a non-substrate. Correct predictions are indicated by bold and large font type. Experimental data [45,46] is included for comparison. ^aStructure was resolved with an inhibitor bound. ^bDisplaced histidine.