# Molecular modelling and docking analysis of a modelled trmB protein from Pseudomonas aeruginosa with selected chemical compounds

**Authors:** Sakshi Bhati, Imteyaz Qamar, Nagendra Singh

PMC · DOI: 10.6026/973206300210657 · Bioinformation · 2025-04-30

## TL;DR

This paper models a protein from Pseudomonas aeruginosa and identifies two chemical compounds that bind well to it, which could help in developing new antimicrobial treatments.

## Contribution

The study identifies two chemical compounds with optimal binding to a modeled trmB protein from Pseudomonas aeruginosa.

## Key findings

- Two compounds (5136 and 9865603) showed optimal binding with the modeled trmB protein.
- The compounds are from a chemical library and are proposed for further antimicrobial development.

## Abstract

Antimicrobial resistance (AMR) threatens global health with rising antibiotic-resistant infections, requiring novel antimicrobial
targets. Therefore, it is of interest to report the molecular modeling and docking analysis trmB from Pseudomonas aeruginosa with
suitable compounds. We show two compounds (5136 and 9865603) from the chemical library have optimal binding with the modelled
trmB from Pseudomonas aeruginosa for further consideration.

## Linked entities

- **Proteins:** trmB (tRNA (guanine-N(7)-)-methyltransferase)
- **Species:** Pseudomonas aeruginosa (taxon 287)

## Full-text entities

- **Diseases:** infections (MESH:D007239)
- **Species:** Pseudomonas aeruginosa (species) [taxon 287]

## Full text

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## References

26 references — full list in the complete paper: https://tomesphere.com/paper/PMC12236524/full.md

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Source: https://tomesphere.com/paper/PMC12236524