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1KTI

BINDING OF 100 MM N-ACETYL-N'-BETA-D-GLUCOPYRANOSYL UREA TO GLYCOGEN PHOSPHORYLASE B: KINETIC AND CRYSTALLOGRAPHIC STUDIES

Replaces:  1K0Q
Summary for 1KTI
Entry DOI10.2210/pdb1kti/pdb
DescriptorGLYCOGEN PHOSPHORYLASE, MUSCLE FORM, N-(acetylcarbamoyl)-beta-D-glucopyranosylamine, PYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total)
Functional Keywordsglycogenolysis, type 2 diabetes, transferase
Biological sourceOryctolagus cuniculus (rabbit)
Total number of polymer chains1
Total formula weight97802.58
Authors
Oikonomakos, N.G.,Kosmopoulou, M.,Zographos, S.E.,Leonidas, D.D.,Chrysina, E.D.,Somsak, L.,Nagy, V.,Praly, J.P.,Docsa, T.,Toth, B.,Gergely, P. (deposition date: 2002-01-16, release date: 2002-01-30, Last modification date: 2020-07-29)
Primary citationOikonomakos, N.G.,Kosmopoulou, M.,Zographos, S.E.,Leonidas, D.D.,Chrysina, E.D.,Somsak, L.,Nagy, V.,Praly, J.P.,Docsa, T.,Toth, B.,Gergely, P.
Binding of N-acetyl-N'-beta-D-glucopyranosyl urea and N-benzoyl-N'-beta-D-glucopyranosyl urea to glycogen phosphorylase b: kinetic and crystallographic studies.
Eur.J.Biochem., 269:1684-1696, 2002
Cited by
PubMed: 11895439
DOI: 10.1046/j.1432-1327.2002.02813.x
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.97 Å)
Structure validation

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