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Structure paper

TitleMolecular insights into the function of RING finger (RNF)-containing proteins hRNF8 and hRNF168 in Ubc13/Mms2-dependent ubiquitylation.
Journal, issue, pagesJ. Biol. Chem., Vol. 287, Page 23900-23910, Year 2012
Publish dateDec 10, 2009 (structure data deposition date)
AuthorsCampbell, S.J. / Edwards, R.A. / Leung, C.C. / Neculai, D. / Hodge, C.D. / Dhe-Paganon, S. / Glover, J.N.
External linksJ. Biol. Chem. / PubMed:22589545
MethodsX-ray diffraction
Resolution2.12 - 4.802 Å
Structure data

PDB-3l11:
Crystal Structure of the Ring Domain of RNF168
Method: X-RAY DIFFRACTION / Resolution: 2.12 Å

PDB-4orh:
Crystal structure of RNF8 bound to the UBC13/MMS2 heterodimer
Method: X-RAY DIFFRACTION / Resolution: 4.802 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MLI:
MALONATE ION

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsLIGASE / E3 Ligase / RING domain / DNA damage / Chromatin regulator / Chromosomal protein / DNA repair / Metal-binding / Nucleus / Phosphoprotein / Ubl conjugation pathway / Zinc-finger / Structural Genomics / Structural Genomics Consortium / SGC / PROTEIN BINDING/LIGASE / COILED-COIL / E3 UBIQUITIN LIGASE / UBIQUITIN / PROTEIN BINDING-LIGASE / PROTEIN BINDING-LIGASE complex

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