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Structure paper

TitleKinetic and crystallographic studies of glucopyranosylidene spirothiohydantoin binding to glycogen phosphorylase B.
Journal, issue, pagesBioorg. Med. Chem., Vol. 10, Page 261-268, Year 2002
Publish dateAug 29, 2000 (structure data deposition date)
AuthorsOikonomakos, N.G. / Skamnaki, V.T. / Osz, E. / Szilagyi, L. / Somsak, L. / Docsa, T. / Toth, B. / Gergely, P.
External linksBioorg. Med. Chem. / PubMed:11741774
MethodsX-ray diffraction
Resolution2.26 - 2.36 Å
Structure data

PDB-1ggn:
Structures of glycogen phosphorylase-inhibitor complexes and the implications for structure-based drug design
Method: X-RAY DIFFRACTION / Resolution: 2.36 Å

PDB-1hlf:
BINDING OF GLUCOPYRANOSYLIDENE-SPIRO-THIOHYDANTOIN TO GLYCOGEN PHOSPHORYLASE B: KINETIC AND CRYSTALLOGRAPHIC STUD
Method: X-RAY DIFFRACTION / Resolution: 2.26 Å

Chemicals

ChemComp-GLS:
BETA-D-GLUCOPYRANOSE SPIROHYDANTOIN

ChemComp-PLP:
PYRIDOXAL-5'-PHOSPHATE

ChemComp-HOH:
WATER

ChemComp-GL4:
(5S,7R,8S,9S,10R)-8,9,10-trihydroxy-7-(hydroxymethyl)-2-thioxo-6-oxa-1,3-diazaspiro[4.5]decan-4-one

Source
  • oryctolagus cuniculus (rabbit)
KeywordsTRANSFERASE / GLYCOGEN PHOSPHORYLASE / INHIBITOR COMPLEX / CATALYTIC SITE / DESIGN

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