A C2HC zinc finger is essential for the activity of the RING ubiquitin ligase RNF125. Determined by X-ray diffraction at 1.55 Å resolution. Released 27 Jul 2016.
Explore 5DKA in 3D Show helices and sheets RCSB PDB PDBe
5DKA contains 12 α-helices and 18 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 |
|---|---|---|---|
| β-strand | 36 | 1 | 1 |
| β-strand | 43 | 1 | 1 |
| α-helix | 44 | 1 | |
| β-strand | 47-49 | 3 | 2 |
| β-strand | 55-57 | 3 | 2 |
| α-helix | 58-67 | 10 | |
| β-strand | 71 | 1 | 3 |
| β-strand | 78 | 1 | 3 |
| β-strand | 84-85 | 2 | 2 |
| α-helix | 87-93 | 7 | |
| β-strand | 97-99 | 3 | 4 |
| β-strand | 106-108 | 3 | 4 |
| α-helix | 109-111 | 3 | |
| α-helix | 112-118 | 7 | |
| α-helix | 120-126 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| E3 ubiquitin-protein ligase RNF125 | A, B | protein | 232 | Homo sapiens | Q96EQ8 (AlphaFold model) |
>5DKA_1 E3 ubiquitin-protein ligase RNF125 (chains A, B) MGSVLSTDSGKSAPASATARALERRRDPELPVTSFDCAVCLEVLHQPVRTRCGHVFCRSC IATSLKNNKWTCPYCRAYLPSEGVPATDVAKRMKSEYKNCAECDTLVCLSEMRAHIRTCQ KYIDKYGPLQELEETAARCVCPFCQRELYEDSLLDHCITHHRSERRPVFCPLCRLIPDEN PSSFSGSLIRHLQVSHTLFYDDFIDFNIIEEALIRRVLDRSLLEYVNHSNTT
Water and common crystallization additives (CL) are not listed.
A C2HC zinc finger is essential for the RING-E2 interaction of the ubiquitin ligase RNF125. Bijlmakers, M.J., Teixeira, J.M., Boer, R. et al. Sci Rep (2016) 6:29232-29232. DOI 10.1038/srep29232 · PubMed
Other PDB entries of the same protein (UniProt Q96EQ8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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