3L11: Ring Domain of RNF168

Crystal Structure of the Ring Domain of RNF168. Determined by X-ray diffraction at 2.12 Å resolution. Released 19 Jan 2010.

Method
X-ray diffraction
Resolution
2.12 Å
Organism
Homo sapiens
Chains
1
Atoms
891
Mol. weight
13.47 kDa
Ligands
ZN, MLI
Released
19 Jan 2010

Explore 3L11 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3L11 contains 8 α-helices and 7 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 8 helices, 7 β-strands

ElementResiduesLengthSheet
α-helix2-43
α-helix7-104
α-helix11-144
β-strand1511
β-strand2211
β-strand27-2822
β-strand34-3522
α-helix37-404
α-helix41-455
β-strand5013
β-strand5713
α-helix59-679
β-strand7212
α-helix74-8310
α-helix85-939

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
E3 ubiquitin-protein ligase RNF168Aprotein115Homo sapiensQ8IYW5 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3L11_1 E3 ubiquitin-protein ligase RNF168 (chains A)
GSMALPKDAIPSLSECQCGICMEILVEPVTLPCNHTLCKPCFQSTVEKASLCCPFCRRRV
SSWTRYHTRRNSLVNVELWTIIQKHYPRECKLRASGQESEEVADDYQPVRLLSKP

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2
MLIMalonate ionC3 H2 O42

Primary citation

Molecular insights into the function of RING finger (RNF)-containing proteins hRNF8 and hRNF168 in Ubc13/Mms2-dependent ubiquitylation. Campbell, S.J., Edwards, R.A., Leung, C.C. et al. J Biol Chem (2012) 287:23900-23910. DOI 10.1074/jbc.M112.359653 · PubMed

Other PDB entries of the same protein (UniProt Q8IYW5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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