Structure of RING finger protein 165. Determined by X-ray diffraction at 1.9 Å resolution. Released 9 Dec 2015.
Explore 5D0I in 3D Show helices and sheets RCSB PDB PDBe
5D0I contains 7 α-helices and 13 β-strands across 2 chains. 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 | 261-264 | 4 | |
| β-strand | 266-269 | 4 | 1 |
| β-strand | 293 | 1 | 2 |
| α-helix | 299 | 1 | |
| β-strand | 300 | 1 | 2 |
| α-helix | 301 | 1 | |
| β-strand | 306-309 | 4 | 1 |
| β-strand | 315-317 | 3 | 1 |
| α-helix | 318-328 | 11 | |
| β-strand | 330 | 1 | 3 |
| β-strand | 337 | 1 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 293 | 1 | 4 |
| β-strand | 300 | 1 | 4 |
| β-strand | 307-309 | 3 | 5 |
| β-strand | 315-317 | 3 | 5 |
| α-helix | 318-327 | 10 | |
| β-strand | 330 | 1 | 6 |
| α-helix | 336 | 1 | |
| β-strand | 337 | 1 | 6 |
| α-helix | 338-339 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| RING finger protein 165 | A, B | protein | 97 | Homo sapiens | Q6ZSG1 (AlphaFold model) |
>5D0I_1 RING finger protein 165 (chains A, B) GPLGSGAVQNTIERFTFPHKYKKRRPQDGKGKKDEGEESDTDEKCTICLSMLEDGEDVRR LPCMHLFHQLCVDQWLAMSKKCPICRVDIETQLGADS
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 4 |
Water and common crystallization additives (SO4) are not listed.
Secondary ubiquitin-RING docking enhances Arkadia and Ark2C E3 ligase activity. Wright, J.D., Mace, P.D., Day, C.L. Nat Struct Mol Biol (2016) 23:45-52. DOI 10.1038/nsmb.3142 · PubMed
Other PDB entries of the same protein (UniProt Q6ZSG1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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