Crystal Structure of the RING domain of RNF168. Determined by X-ray diffraction at 2.6 Å resolution. Released 10 Jul 2013.
Explore 4GB0 in 3D Show helices and sheets RCSB PDB PDBe
4GB0 contains 6 α-helices and 6 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 | 12-14 | 3 | |
| β-strand | 15 | 1 | 1 |
| β-strand | 22 | 1 | 1 |
| β-strand | 26-28 | 3 | 2 |
| β-strand | 34-36 | 3 | 2 |
| α-helix | 37-39 | 3 | |
| α-helix | 40-48 | 9 | |
| β-strand | 50 | 1 | 3 |
| β-strand | 57 | 1 | 3 |
| α-helix | 59-67 | 9 | |
| α-helix | 74-83 | 10 | |
| α-helix | 85-92 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| E3 ubiquitin-protein ligase RNF168 | A | protein | 121 | Homo sapiens | Q8IYW5 (AlphaFold model) |
>4GB0_1 E3 ubiquitin-protein ligase RNF168 (chains A) MGHHHHHHGSMALPKDAIPSLSECQCGICMEILVEPVTLPCNHTLCKPCFQSTVEKASLC CPFCRRRVSSWTRYHTRRNSLVNVELWTIIQKHYPRECKLRASGQESEEVADDYQPVRLL S
Structural basis for role of ring finger protein RNF168 RING domain. Zhang, X.Q., Chen, J., Wu, M. et al. Cell Cycle (2013) 12:312-321. DOI 10.4161/cc.23104 · 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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