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TitleEvidence for an active T-state pig kidney fructose 1,6-bisphosphatase: interface residue Lys-42 is important for allosteric inhibition and AMP cooperativity.
Journal, issue, pagesProtein Sci., Vol. 5, Page 2333-2342, Year 1996
Publish dateAug 24, 1996 (structure data deposition date)
AuthorsLu, G. / Stec, B. / Giroux, E.L. / Kantrowitz, E.R.
External linksPubMed:8931152
MethodsX-ray diffraction
Resolution2.3 Å
Structure data

PDB-1fsa:
THE T-STATE STRUCTURE OF LYS 42 TO ALA MUTANT OF THE PIG KIDNEY FRUCTOSE 1,6-BISPHOSPHATASE EXPRESSED IN E. COLI
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-F6P:
6-O-phosphono-beta-D-fructofuranose

ChemComp-MN:
Unknown entry

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

ChemComp-HOH:
WATER

Source
  • sus scrofa (pig)
KeywordsHYDROLASE / LYASE / FRUCTOSE 1 / 6-BISPHOSPHATASE / CARBOHYDRATE METABOLISM / GLUCONEOGENESIS / ACETYLATION PHOSPHORYLATION

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