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Structure paper

TitleSubstitutions at a rheostat position in human aldolase A cause a shift in the conformational population.
Journal, issue, pagesProtein Sci., Vol. 31, Page 357-370, Year 2022
Publish dateJun 30, 2020 (structure data deposition date)
AuthorsFenton, K.D. / Meneely, K.M. / Wu, T. / Martin, T.A. / Swint-Kruse, L. / Fenton, A.W. / Lamb, A.L.
External linksProtein Sci. / PubMed:34734672
MethodsX-ray diffraction
Resolution1.88 - 2.6 Å
Structure data

PDB-6xmh:
Human aldolase A wild type
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-6xml:
Human aldolase A I98C
Method: X-RAY DIFFRACTION / Resolution: 1.88 Å

PDB-6xmm:
Human aldolase A I98S
Method: X-RAY DIFFRACTION / Resolution: 2.11 Å

PDB-6xmo:
Human aldolase A I98F
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsLYASE / rheostat / allosterism

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