Journal:Acta Cryst F:S2053230X18018083
From Proteopedia
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One complex has a well-ordered ligand in a catalytic site and the model provides an improved description of enzyme-inhibitor interactions ([[1dib]]: <scene name='80/804503/Cv/2'>L34</scene>). One ligand may adopt two conformations in the binding site rather than the single one previously described ([[1dia]]: <scene name='80/804503/Cv/3'>L24</scene>; 1st conformation is colored in wheat and 2nd conformation is in pink). There is no evidence to support incorporation of the third compound in the model ([[1dig]]:L37). Our interpretation of the data supports a correlation between the models and inhibition activity for two of the compounds. In the case of the third, inconsistencies are noted that would need to be addressed by further work. | One complex has a well-ordered ligand in a catalytic site and the model provides an improved description of enzyme-inhibitor interactions ([[1dib]]: <scene name='80/804503/Cv/2'>L34</scene>). One ligand may adopt two conformations in the binding site rather than the single one previously described ([[1dia]]: <scene name='80/804503/Cv/3'>L24</scene>; 1st conformation is colored in wheat and 2nd conformation is in pink). There is no evidence to support incorporation of the third compound in the model ([[1dig]]:L37). Our interpretation of the data supports a correlation between the models and inhibition activity for two of the compounds. In the case of the third, inconsistencies are noted that would need to be addressed by further work. | ||
| - | + | <scene name='80/804503/Cv/10'>Methylenetetrahydrofolate dehydrogenase/cyclohydrolase interactions with the inhibitor L34</scene>. Water molecule is shown as red sphere. Distance measurements (in Å) are represented as white dashed lines. | |
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 10:56, 23 December 2018
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