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Fig. 4 a Binding site of bound chain (PDB ID: 5p2p, CHAIN ID: A).
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The ATP binding site of ERK1 is bound by the MAPK inhibitor 5-iodotubericidin, colored yellow.
The nucleoside-binding site of vcCNT bound to zebularine is shown in stereo in stick representation in the same orientation and colored as in Figure 2A.
4– 6 AIs are characterized into two types: steroidal aromatase inactivators, which bind irreversibly to the androstenedione binding site of aromatase, and nonsteroidal AIs, which bind in a reversible fashion to the heme component of aromatase.
Molecular docking results showed that most of these compounds bind in the binding site of BCRP at the interface between the membrane and outer environment.
These ligands bind to colchicine binding site of tubulin near the α- and β-tubulin interface and interfere with tubulin polymerization.
The results showed that all of these compounds bind to the binding site of BCRP with relatively suitable binding energies and therefore could be potential inhibitors of both αβ-tubulin and BCRP proteins.
Both VHH competed with sialylglycoprotein fetuin, which binds the receptor binding site of hemagglutinin 5 (Fig. 3B).
ATP analogs, which bind to ATP binding site of DDX3X, were shown to inhibit HIV-1 replication [42].
These latter molecules bind the myristate binding site of ABL, as opposed to the ATP binding site targeted by imatinib and related inhibitors.
Examination of an X-ray crystal structure of 6 bound to the ATP binding site of Chk1 reveals that the hydroxyl group binds oriented into a pocket, which is too small to accommodate a substituent such as the 4-nitrobenzyl group.
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