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Table 5 Docking of acetylcholine and butyrylcholine

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

 

Docking into:

 

X-ray structures

Substrate-imprinted structures

Structure

ACh

BuCh

ACh

BuCh

Torpedo californica acetylcholine esterase

Experimental data

+

-

+

-

1CFJa

+

+

+

-

1DX6a

+

+

+

+

1E3Qa

-

-

+

-

1EVEa

+

+

+

-

1VXRa, b

-

-

-

-

1QIM

+

+

+

-

No. false predictions

2

4

1

1

human butyrylcholine esterase

Experimental data

+

+

+

+

1P0M

-

-

-

-

1XLUa

+

+

+

+

1XLVa

+

+

+

+

1XLWa

-

-

+

+

No. false predictions

2

2

1

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.