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TitleThe design and optimization of a series of 2-(pyridin-2-yl)-1H-benzimidazole compounds as allosteric glucokinase activators.
Journal, issue, pagesBioorg. Med. Chem., Vol. 17, Page 7042-7051, Year 2009
Publish dateApr 14, 2009 (structure data deposition date)
AuthorsTakahashi, K. / Hashimoto, N. / Nakama, C. / Kamata, K. / Sasaki, K. / Yoshimoto, R. / Ohyama, S. / Hosaka, H. / Maruki, H. / Nagata, Y. ...Takahashi, K. / Hashimoto, N. / Nakama, C. / Kamata, K. / Sasaki, K. / Yoshimoto, R. / Ohyama, S. / Hosaka, H. / Maruki, H. / Nagata, Y. / Eiki, J. / Nishimura, T.
External linksBioorg. Med. Chem. / PubMed:19736020
MethodsX-ray diffraction
Resolution2.11 Å
Structure data

PDB-3h1v:
Human glucokinase in complex with a synthetic activator
Method: X-RAY DIFFRACTION / Resolution: 2.11 Å

Chemicals

ChemComp-GLC:
alpha-D-glucopyranose

ChemComp-TK1:
1-({5-[4-(methylsulfonyl)phenoxy]-2-pyridin-2-yl-1H-benzimidazol-6-yl}methyl)pyrrolidine-2,5-dione

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / glucokinase / diabetes / allosteric activator / Alternative splicing / ATP-binding / Diabetes mellitus / Disease mutation / Glycolysis / Kinase / Nucleotide-binding / Polymorphism

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