Crystal Structure of the Ring Domain of RNF168. Determined by X-ray diffraction at 2.12 Å resolution. Released 19 Jan 2010.
Explore 3L11 in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-4 | 3 | |
| α-helix | 7-10 | 4 | |
| α-helix | 11-14 | 4 | |
| β-strand | 15 | 1 | 1 |
| β-strand | 22 | 1 | 1 |
| β-strand | 27-28 | 2 | 2 |
| β-strand | 34-35 | 2 | 2 |
| α-helix | 37-40 | 4 | |
| α-helix | 41-45 | 5 | |
| β-strand | 50 | 1 | 3 |
| β-strand | 57 | 1 | 3 |
| α-helix | 59-67 | 9 | |
| β-strand | 72 | 1 | 2 |
| α-helix | 74-83 | 10 | |
| α-helix | 85-93 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| E3 ubiquitin-protein ligase RNF168 | A | protein | 115 | Homo sapiens | Q8IYW5 (AlphaFold model) |
>3L11_1 E3 ubiquitin-protein ligase RNF168 (chains A) GSMALPKDAIPSLSECQCGICMEILVEPVTLPCNHTLCKPCFQSTVEKASLCCPFCRRRV SSWTRYHTRRNSLVNVELWTIIQKHYPRECKLRASGQESEEVADDYQPVRLLSKP
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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