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Figure 6 | BMC Bioinformatics

Figure 6

From: ResBoost: characterizing and predicting catalytic residues in enzymes

Figure 6

ResBoost's catalytic residue predictions for dihydroneopterin aldolase from Staphylococcus aureus(PDB ID: 2dhn). Results are shown for sensitivity/specificity trade-off parameter k = 256 and k = 350. ResBoost at k = 256 correctly predicts the known catalytic residues, Glu22 and Lys100, resulting in no false negatives. ResBoost also predicts Glu74, which though not listed as a catalytic residue in the CSA, exhibits a dramatic change in the affinities of the enzyme for the substrate or product analogues when mutated. At k = 350, ResBoost is more sensitive and detects residues located in a cleft away from the active site. Of these predicted residues, Tyr54 functions with Glu22 and Lys100 in organizing the catalytic center assembly while some of the other residues (Val48, Thr51, Val52, His53) are involved in electrostatic or hydrophobic interactions with the ligand in the crystal structure with neopterin (NP), an analog of 7,8-dihydroneopterin (DHNP) [28].

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