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Article

The Impact of Second-Shell Residues on Substrate Binding at the Active Site of Thymidylate Synthase from Mycobacterium tuberculosis.

The journal of physical chemistry. B - 2 Jul 2026

Sengupta Pallav, Satpati Priyadarshi

Abstract excerpt

Employing classical alchemical free-energy simulations, we quantitatively evaluated how mutations in second-shell residues (Y44, Q106, Y108, and T181) affect the energetics of substrate (dUMP) binding to the active site of MtbThyX, an important drug target for Mycobacterium tuberculosis. The substrate binding affinity of nine mutants was compared with the wild-type MtbThyX. We found that specific mutations (viz.,...

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PMID: 42322289
DOI: 10.1021/acs.jpcb.6c01496

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

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