Ternary structure of Plasmodium vivax N-myristoyltransferase with myristoyl-CoA and inhibitor IMP-0001173

Bolling, C.; Mendez, A.; Taylor, S.; Makumire, S.; Reers, A.; Zigweid, R.; Subramanian, S.; Dranow, D.M.; Staker, B.; Edwards, T.E.; Tate, E.W.; Bell, A.S.; Myler, P.J.; Asojo, O.A.; Chakafana, G.

doi:10.1107/S2053230X24008604

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 2
Myr-CoA and inhibitor (IMP-0001173) binding by PvNMT. The interactions were analyzed with Discovery Studio Visualizer (https://discover.3ds.com/discovery-studio-visualizer). (a) Stick representation of amino-acid residues (gray) interacting with Myr-CoA (green). (b) The Myr-CoA-binding pocket is slightly positively charged [shown in the same view as in (a)]. (c) The inhibitor IMP-0001173 (shown in cyan) interacts with amino acids (gray). (d) IMP-0001173 has primarily electrostatic interactions in the peptide-binding pocket.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 80| Part 10| October 2024| Pages 269-277

https://doi.org/10.1107/S2053230X24008604

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