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Structure paper

TitleThe origin and evolution of human glutaminases and their atypical C-terminal ankyrin repeats.
Journal, issue, pagesJ. Biol. Chem., Vol. 292, Page 11572-11585, Year 2017
Publish dateNov 24, 2016 (structure data deposition date)
AuthorsPasquali, C.C. / Islam, Z. / Adamoski, D. / Ferreira, I.M. / Righeto, R.D. / Bettini, J. / Portugal, R.V. / Yue, W.W. / Gonzalez, A. / Dias, S.M.G. / Ambrosio, A.L.B.
External linksJ. Biol. Chem. / PubMed:28526749
MethodsX-ray diffraction
Resolution1.423 - 3.6 Å
Structure data

PDB-5u0i:
C-terminal ankyrin repeats from human kidney-type glutaminase (KGA) - tetragonal crystal form
Method: X-RAY DIFFRACTION / Resolution: 1.423 Å

PDB-5u0j:
C-terminal ankyrin repeats from human kidney-type glutaminase (KGA) - monoclinic crystal form
Method: X-RAY DIFFRACTION / Resolution: 1.72 Å

PDB-5u0k:
C-terminal ankyrin repeats from human liver-type glutaminase (GAB/LGA)
Method: X-RAY DIFFRACTION / Resolution: 2.548 Å

PDB-5uqe:
Multidomain structure of human kidney-type glutaminase(KGA/GLS)
Method: X-RAY DIFFRACTION / Resolution: 3.6 Å

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-04A:
N,N'-[sulfanediylbis(ethane-2,1-diyl-1,3,4-thiadiazole-5,2-diyl)]bis(2-phenylacetamide)

Source
  • homo sapiens (human)
KeywordsHYDROLASE / Glutaminase / ankyrin / human / GLS1 / GLS2 / kidney-type / KGA / GLS

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