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

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

Residue Structural features	Binding Sites	Non-binding Sites
Ordered^a	98.0%	91.9%
Disordered^a	2.0%	8.1%
Ordered^b	97.8%	91.9%
Disordered^b	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%

ISSN: 1471-2105