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Table 2 Comparisons of residue structural features between real binding sites and those normal ones in ATP168 and ATP227

From: Predicting protein-ATP binding sites from primary sequence through fusing bi-profile sampling of multi-view features

Residue Structural features Binding Sites Non-binding Sites
Ordereda 98.0% 91.9%
Disordereda 2.0% 8.1%
Orderedb 97.8% 91.9%
Disorderedb 2.2% 8.1%
Coil (C)a 49.6% 41.7%
Helical (H)a 26.0% 40.3%
Strand (E)a 24.4% 18.0%
Coil (C)b 49.3% 41.7%
Helical (H)b 24.6% 40.4%
Strand (E)b 26.1% 17.9%
Exposed (E)a 24.7% 41.5%
Buried (B)a 75.3% 58.5%
Exposed (E)b 21.3% 41.5%
Buried (B)b 78.7% 58.5%
  1. a Statistics on ATP168 dataset.
  2. b Statistics on ATP227 dataset.