Skip to main content

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.)