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Structure paper

TitleAllosteric Fbpase Inhibitors Gain 10(5) Times in Potency When Simultaneously Binding Two Neighboring AMP Sites.
Journal, issue, pagesBioorg. Med. Chem. Lett., Vol. 18, Page 4708-, Year 2008
Publish dateApr 9, 2008 (structure data deposition date)
AuthorsHebeisen, P. / Kuhn, B. / Kohler, P. / Gubler, M. / Huber, W. / Kitas, E. / Schott, B. / Benz, J. / Joseph, C. / Ruf, A.
External linksBioorg. Med. Chem. Lett. / PubMed:18650089
MethodsX-ray diffraction
Resolution2 - 2.2 Å
Structure data

PDB-2jjk:
FRUCTOSE-1,6-BISPHOSPHATASE(D-FRUCTOSE-1,6-BISPHOSPHATE -1- PHOSPHOHYDROLASE) (E.C.3.1.3.11) COMPLEXED WITH A DUAL BINDING AMP SITE INHIBITOR
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-2vt5:
FRUCTOSE-1,6-BISPHOSPHATASE(D-FRUCTOSE-1,6-BISPHOSPHATE -1- PHOSPHOHYDROLASE) (E.C.3.1.3.11) COMPLEXED WITH A DUAL BINDING AMP SITE INHIBITOR
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-R15:
N,N'-(heptane-1,7-diyldicarbamoyl)bis(3-chlorobenzenesulfonamide)

ChemComp-HOH:
WATER

ChemComp-ROK:
4-AMINO-N-[(2-SULFANYLETHYL)CARBAMOYL]BENZENESULFONAMIDE

Source
  • homo sapiens (human)
KeywordsHYDROLASE / HYDROLASE (PHOSPHORIC MONOESTER) / DISEASE MUTATION / ALLOSTERIC ENZYME / ZINC / POLYMORPHISM / GLUCONEOGENESIS / CARBOHYDRATE METABOLISM

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