Playing 37 and 89 sequence identity and coverage, respecprotein from Escherichia coli displaying
Playing 37 and 89 sequence identity and coverage, respecprotein from Escherichia coli displaying 37 and 89 sequence identity and coverage, tively (Figure 7). The modelmodel was refined (process section)its structural quality was respectively (Figure 7). The was refined (process section) and and its structural top quality assessed prior to andand right after the optimization procedure (Table 5). Theoptimization helped was assessed before following the optimization procedure (Table five). The optimization helped to improve the high quality on the model, creating it compatible using the UCB-5307 References template evaluation. to improve the excellent from the model, generating it compatible together with the template evaluation. The MolProbity score was greater for the refined model than for the template, with values The MolProbity score was much better for refined of 0.88 and 0.98, respectively. A score equal to zero represents the structure possessing no of 0.88 and 0.98, respectively. A score equal to zero represents the structure stereochemical troubles. The model’s QMEAN had a reduce score than the template ((-2.39 QMEAN had a reduced score than the template -2.39 stereochemical challenges. and 0.02, respectively). Nonetheless, this value was compatible with high-quality models, and 0.02, respectively). Nevertheless, this value was compatible with high-quality models, producing it appropriate for making it appropriate for subsequent analysis.Biomolecules 2021, 11, x FOR PEER Overview Biomolecules 2021, 11, 1486 PEER Review Biomolecules 2021, 11, x FOR13 of 21 13 of 21 12 ofFigure 7. Pairwise sequence alignment employed for the comparative modeling in the J. curcas esterase primarily based on the strucFigure 7. Pairwise sequence alignment employed for the comparative modeling in the J. curcas esterase based around the ture on the uncharacterized protein from E. coli O157:H7 str. Sakai (PDB ID: 4ZV9). The sequences have 37 identity and Figure 7. Pairwise sequence alignment employedcoli O157:H7 str. Sakai (PDB ID: 4ZV9). curcas esterase and template. Black structure of the The active web-site residues–Cys-78, Asp-126, and His-161- are conservedJ.(Z)-Semaxanib In stock involving target based 37 identity 89 coverage. uncharacterized protein from E. for the comparative modeling of your The sequences have on the structure 89 coverage.the sequence alignment represent identical residues. Points representsequences have 37 identity and and ofpositions within the active internet site residues–Cys-78, Asp-126, and His-161-4ZV9). The gaps. filled the uncharacterized protein from E. coli O157:H7 str. Sakai (PDB ID: are conserved involving target and template. 89 coverage. The active web page residues–Cys-78, represent and His-161- are conserved between target and template. Black Black filled positions within the sequence alignment Asp-126, identical residues. Points represent gaps. filled positions in the sequence alignment represent identical residues. Points represent gaps. Table five. Evaluation of J. curcas esterase model and its template. Table 5. Evaluation of J. curcas esterase model and its template. Table five. Evaluation of J. curcas esterase model and its template. PDB ID: Model Assessment Model PDB ID: Model 4ZV9 Refined Assessment Model PDB ID: Model 4ZV9 RefinedMolProbity Score Clash Score Ramachandran Favoured Ramachandran Outliers Rotamer Outliers QMEANAssessment Model MolProbity Score 0.98 1.72 0.88 4ZV9 0.98 Score 1.72 0.88Refined Clash 1.37 four.62 0.00 MolProbity Score 0.98 1.72 1.37 4.62 0.00 0.88 Ramachandran Favoured 97.42 91.92 94.44 97.42 91.92 94.44 0.00 Clash Score 1.37 4.62 Ramachandran Outl.