6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase
From Proteopedia
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Three loop regions surround the HPPK active site. Upon binding of ATP, the <scene name='59/593854/Cv/2'>flexible loops</scene> region (purple) changes its conformation and enables the binding of HMDP. <scene name='59/593854/Cv/6'>Active site</scene>. Water molecules are shown as red spheres. | Three loop regions surround the HPPK active site. Upon binding of ATP, the <scene name='59/593854/Cv/2'>flexible loops</scene> region (purple) changes its conformation and enables the binding of HMDP. <scene name='59/593854/Cv/6'>Active site</scene>. Water molecules are shown as red spheres. | ||
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| + | ==3D structures of HPPK== | ||
| + | [[HPPK 3D structures]] | ||
</StructureSection> | </StructureSection> | ||
Revision as of 09:07, 21 February 2019
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3D structures of HPPK
Updated on 21-February-2019
References
- ↑ Xiao B, Shi G, Chen X, Yan H, Ji X. Crystal structure of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, a potential target for the development of novel antimicrobial agents. Structure. 1999 May;7(5):489-96. PMID:10378268
