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Interactions of serotonin with amino-acid residues of the binding pocket are shown in Fig 2C.
The peptide backbone is in colored ribbon diagram, the metal ions in the PP1G active site are shown as pink spheres whereas latrunculin B and ATP in the actin nucleotide binding pocket are shown in stick diagram (blue and green respectively).
The crystal structure of 5HTBP-gran (complex with granisetron) was solved from diffraction data to a resolution of 2.4 Å. Simple electron density for granisetron is shown as a green mesh (1.5σ, Fig 2B) and side-chain interactions with residues in the binding pocket are shown in Fig 2D.
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Docked ligand conformation, is presented with sticks and the binding pocket is shown as surface.
Further, a loop toward the back end of the uracil binding pocket is shown to flexibly adjust to the varying chemistry of different compounds through an "induced-fit" association mechanism that was not observed in earlier hUPP1 structures.
Side chains of residues lining the binding pockets are shown as sticks and are numbered.
f, g, Ribbon diagrams of the resetting state (f) and engaged state (g) nucleotide binding pockets are shown for each protomer.
The strong binding metabolites of the respective AoXlnR and AoAmyR binding pockets are shown in Fig. 5.
For comparison, the binding pockets are shown: YePEPT (A and D); GkPOTE310Q (B and E); and PepTSt (C and F).
(A ) The C. thermophilum LIC was aligned with Ras-GMPPNP (PDB 5P21) and a view of the GTP-binding pocket is shown with corresponding G motifs labeled.
A region corresponding to the Chd1 ATP-binding pocket is shown below and aligned to various homologues from Saccharomyces cerevisiae and Drosophila melanogaster.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com