Table 1 Hydrogen bonds formed between inhibitors (Cantharidin, Norcantharidin and Endothall) and PP5c during MD simulationsa.

From: Insights into the key interactions between human protein phosphatase 5 and cantharidin using molecular dynamics and site-directed mutagenesis bioassays

System

DONOR

ACCEPTORH

ACCEPTOR

Occupancy(%)

Distance (Å)

Angle (°)

res@atom

res@atom

res@atom

Cantharidin-PP5c

 

318@O5

225@HH11

225@NH1

97.09

2.82 (0.12)

33.19 (11.71)

 

318@O4

129@HE2

129@NE2

60.03

2.77 (0.11)

40.23 (13.50)

Norcantharidin-PP5c

 

318@O5

225@HH11

225@NH1

93.41

2.77 (0.11)

31.60 (12.35)

 

318@O3

129@HE2

129@NE2

70.47

2.77 (0.12)

41.20 (11.81)

 

318@O4

129@HE2

129@NE2

19.05

3.13 (0.19)

53.5 (5.38)

Endothall-PP5c

 

318@O5

254@H

254@N

69.84

2.92 (0.15)

41.01 (11.88)

 

318@O3

225@HH11

225@NH1

63.22

2.87 (0.20)

26.45 (10.24)

  1. aThe percentage of simulation snapshots (saved every 10 ps) in which the H-bond was present are listed.
  2. Hydrogen bonds are determined by an acceptor/donor atom distance of less than 3.5 Å and an acceptor/H–donor angle of greater than 120°. The occupancy of H-bonds that are formed between the inhibitors and the PP5c larger than 5% is listed.
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