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Structure paper

TitleStructural studies of human muscle FBPase
Journal, issue, pagesTo Be Published
Publish dateMay 23, 2016 (structure data deposition date)
AuthorsBarciszewski, J. / Szpotkowski, K. / Wisniewski, J. / Kolodziejczyk, R. / Jaskolski, M. / Rakus, D. / Dzugaj, A.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.717 - 2.302 Å
Structure data

PDB-5k54:
Human muscle fructose-1,6-bisphosphatase E69Q mutant in active R-state
Method: X-RAY DIFFRACTION / Resolution: 1.717 Å

PDB-5k55:
Human muscle fructose-1,6-bisphosphatase E69Q mutant in active R-state in complex with fructose-6-phosphate
Method: X-RAY DIFFRACTION / Resolution: 1.977 Å

PDB-5k56:
Human muscle fructose-1,6-bisphosphatase in active R-state in complex with fructose-1,6-bisphosphate
Method: X-RAY DIFFRACTION / Resolution: 2.198 Å

PDB-5l0a:
Human muscle fructose-1,6-bisphosphatase E69Q mutant in active R-state in complex with fructose-1,6-bisphosphate
Method: X-RAY DIFFRACTION / Resolution: 2.302 Å

Chemicals

ChemComp-HOH:
WATER

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

ChemComp-FBP:
1,6-di-O-phosphono-beta-D-fructofuranose

Source
  • homo sapiens (human)
KeywordsHYDROLASE / carbohydrate metabolism / glyconeogenesis / muscle izozyme / FBPase / R-state / Leucine lock / E69Q mutant / F6P / F16BP / muscle izoenzyme / E69Q / fructose-1 / 6-bisphosphate

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