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Table 3 Residues in correctly predicted 3 top-ranked clusters

From: Prediction of functionally important residues in globular proteins from unusual central distances of amino acids

Structure Function Cluster
1ahc A (RNA) glycosidase R ¯ , E ¨ ¯ , E ¨ , Q ¯
1bbs A proteinase D ¨ ¯ , D ¨ ¯
1bya A O-glycosidase E ¨ ¯ , R ¯ , E ¨ ¯ , P
1cge A metalloproteinase E ¨ ¯
1djb A hydrolase (β-lactamase) K ¯ , E ¯
1hsi A protease (HIV-2 retropepsin) I ¯ ( flaps )
1hxf H (serine) protease D ¨ ¯
1ifb A fatty acid binding R ¨ , E
1ime A (inositol) phosphatase D ¨ ¯ , D ¨ ¯ , D ¨ ¯
1krn A hydrolase (fibrinolysin) K ¨
1l3f E proteolysin E ¯
1nna A O-glycosidase K ¨ ¯ , E ¨ ¯ , R ¯ , E ¨ ¯ , Q ¯
1npc A (metallo)protease E ¯ , E ¯
1pdy A enolase K ¯ , R ¯ , Q ¯
1psn A (acid) proteinase D ¨ ¯ , D ¨ ¯
1pts A azobenzoic acid binding D ¯
1qif A (acetylcholin)esterase E ¨ ¯
1stn A (phosphodi)esterase R ¯ , D ¨ ¯
1ypi A (triosephosphate) isomerase K ¯ , E ¯
2cba A lyase (anhydrase) E ¨ ¯ , E ¨ ¯
2ctb A hydrolase (carboxypeptidase) E ¯
2fbp B (fructose bis)phosphatase K ¯ , E ¨ ¯ , D ¯ , D ¨ ¯ , E ¨ ¯
2sil A hydrolase (neuraminidase) E ¨ ,Q,Q , R ¨ ¯ , R ¨ ¯
3app A (acid) proteinase D ¨ ¯
3p2p A (carboxyl)esterase R , D ¯
3ptn A hydrolase (tripsin) D ¯
3tms A (methyl)transferase E ¨ ¯ , N ¯ , Q ¯
5dfr A (folic acid) reductase D ¯
8adh A dehydrogenase E ¯ , D ¨ ¯
8rat A hydrolase (ribonuclease) K ¨ ¯ , Q
  1. Residues are sorted in rows according to decreasing unexpectedness. Residues of the highest evolutionary conservation scores according to the ConSurf-DB [66] are underlined; residues indicated as functional by Thematics [25] have overbars; bold residues are annotated as catalytic in the Catalytic Sites Atlas (CSA) [58]. (Two chains of non-enzymatic functions are unannotated in the CSA.)