Modelling substrate specificity and enantioselectivity for lipases and esterases by substrate-imprinted docking

BMC Structural Biology

Table 4 Docking of 2-hydroxyoctanoic acid butyl esters

	Docking into:
	X-ray structures		Substrate-imprinted structures
Structure	(R)-2-HOB	(S)-2-HOB	(R)-2-HOB	(S)-2-HOB
Candida rugosa lipase
Experimental data	+	+	+	+
1CLE^a	+	+	+	+
1CRL	+	+	+	+
1LPM^a	+	+	+	+
1LPN^{a, b}	-	-	-	-
1LPO^a	+	+	+	+
1LPP^{a, b}	-	-	-	-
1LPS^a	-	-	-	+
No. false predictions	3	3	3	2
Burkholderia cepacia lipase
Experimental data	+	+	+	+
2LIP	-	-	-	+
3LIP	-	-	+	-
4LIP^a	+	+	+	+
5LIP^a	+	+	+	+
1OIL	+	+	+	+
1YS1^a	+	+	+	+
1YS2^a	+	+	+	+
No. false predictions	2	2	1	1

Docking of (R)-2-HOB and (S)-2-HOB into seven BCL and seven CRL structures 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 (R)-2-HOB or (S)-2-HOB to be a substrate or a non-substrate. Correct predictions are indicated by bold and large font type. Experimental data [42] is included for comparison. ^aStructure was resolved with an inhibitor bound. ^bDisplaced histidine.

ISSN: 1472-6807