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TitleDomain alternation and active site remodeling are conserved structural features of ubiquitin E1.
Journal, issue, pagesJ. Biol. Chem., Vol. 292, Page 12089-12099, Year 2017
Publish dateJan 26, 2017 (structure data deposition date)
AuthorsLv, Z. / Yuan, L. / Atkison, J.H. / Aldana-Masangkay, G. / Chen, Y. / Olsen, S.K.
External linksJ. Biol. Chem. / PubMed:28572513
MethodsX-ray diffraction
Resolution2.794 Å
Structure data

PDB-5um6:
Crystal Structure of S. pombe Uba1 in a closed conformation
Method: X-RAY DIFFRACTION / Resolution: 2.794 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-8EA:
N-(2-{[(4-chlorophenyl)methyl]disulfanyl}ethyl)decan-1-amine

ChemComp-8E7:
2-(decylamino)ethane-1-thiol

Source
  • schizosaccharomyces pombe (strain 972 / atcc 24843) (yeast)
Keywordsligase/ligase inhibitor / ROSSMANN-LIKE FOLD / UBIQUITIN-LIKE FOLD / UBIQUITIN ACTIVATING ENZYME / ATP BINDING / LIGASE ACTIVITY / ATP/MG BINDING / UBIQUITIN E2 BINDING / LIGASE / TRANSFERASE / ligase-ligase inhibitor complex

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