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Structure paper

TitleStructure of LNX1:Ubc13~Ubiquitin Complex Reveals the Role of Additional Motifs for the E3 Ligase Activity of LNX1.
Journal, issue, pagesJ. Mol. Biol., Vol. 430, Page 1173-1188, Year 2018
Publish dateNov 21, 2016 (structure data deposition date)
AuthorsNayak, D. / Sivaraman, J.
External linksJ. Mol. Biol. / PubMed:29496391
MethodsX-ray diffraction
Resolution1.7 - 3.49 Å
Structure data

PDB-5h7r:
Structural basis of the flanking zinc-finger motifs crucial for the E3 ligase activity of the LNX1 RING domain
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-5h7s:
Structural basis of the flanking zinc-finger motifs crucial for the E3 ligase activity of the LNX1 RING domain
Method: X-RAY DIFFRACTION / Resolution: 3.49 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsLIGASE / RING / Ubiquitination / E3 ligase / Zn finger motif / PROTEIN BINDING/LIGASE/TRANSFERASE / ubiquitin / zinc finger motif / PROTEIN BINDING-LIGASE-TRANSFERASE complex

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