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Structure paper

TitleStructural basis for the activation of acid ceramidase.
Journal, issue, pagesNat Commun, Vol. 9, Page 1621-1621, Year 2018
Publish dateDec 13, 2016 (structure data deposition date)
AuthorsGebai, A. / Gorelik, A. / Li, Z. / Illes, K. / Nagar, B.
External linksNat Commun / PubMed:29692406
MethodsX-ray diffraction
Resolution1.4 - 2.5 Å
Structure data

PDB-5u7z:
Human acid ceramidase (ASAH1, aCDase) self-activated
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-5u81:
Acid ceramidase (ASAH1, aCDase) from naked mole rat, Cys143Ala, uncleaved
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

PDB-5u84:
Acid ceramidase (ASAH1, aCDase) from common minke whale, Cys143Ala, uncleaved
Method: X-RAY DIFFRACTION / Resolution: 2.34 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-CL:
Unknown entry

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-1PE:
PENTAETHYLENE GLYCOL / precipitant*YM

ChemComp-I3C:
5-amino-2,4,6-triiodobenzene-1,3-dicarboxylic acid

ChemComp-IOD:
IODIDE ION

Source
  • homo sapiens (human)
  • heterocephalus glaber (naked mole-rat)
  • balaenoptera acutorostrata (minke whale)
KeywordsHYDROLASE / ceramidase / ceramide / ntn-hydrolase

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