Structure of RNF125 in complex with a UbcH5b~Ub conjugate. Determined by X-ray diffraction at 2.39 Å resolution. Released 19 Jul 2023.
Explore 8GCB in 3D Show helices and sheets RCSB PDB PDBe
8GCB contains 13 α-helices and 17 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 | 1-15 | 15 | |
| β-strand | 21-26 | 6 | 1 |
| β-strand | 29-38 | 10 | 1 |
| α-helix | 39-40 | 2 | |
| β-strand | 49-55 | 7 | 1 |
| α-helix | 64-65 | 2 | |
| β-strand | 66-69 | 4 | 1 |
| β-strand | 75 | 1 | 2 |
| β-strand | 78 | 1 | 2 |
| β-strand | 83 | 1 | 1 |
| β-strand | 84 | 1 | 2 |
| α-helix | 87-89 | 3 | |
| α-helix | 99-111 | 13 | |
| α-helix | 121-129 | 9 | |
| α-helix | 131-145 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 36 | 1 | 3 |
| β-strand | 43 | 1 | 3 |
| α-helix | 44 | 1 | |
| β-strand | 47-49 | 3 | 4 |
| β-strand | 55-57 | 3 | 4 |
| α-helix | 58-67 | 10 | |
| β-strand | 71 | 1 | 5 |
| β-strand | 78 | 1 | 5 |
| β-strand | 84-85 | 2 | 4 |
| α-helix | 87-93 | 7 | |
| β-strand | 97-99 | 3 | 6 |
| β-strand | 106-108 | 3 | 6 |
| α-helix | 109-111 | 3 | |
| α-helix | 112-117 | 6 | |
| α-helix | 120-125 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin-conjugating enzyme E2 D2 | A | protein | 152 | Homo sapiens | P62837 (AlphaFold model) |
| E3 ubiquitin-protein ligase RNF125 | B | protein | 101 | Homo sapiens | Q96EQ8 (AlphaFold model) |
>8GCB_1 Ubiquitin-conjugating enzyme E2 D2 (chains A) GPLGSMALKRIHKELNDLARDPPAQSRAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIH FPTDYPFKPPKVAFTTRIYHPNINSNGSIKLDILRSQWSPALTISKVLLSISSLLSDPNP DDPLVPEIARIYKTDREKYNRIAREWTQKYAM
>8GCB_2 E3 ubiquitin-protein ligase RNF125 (chains B) GPLGSVTSFDCAVCLEVLHQPVRTRCGHVFCRSCIATSLKNNKWTCPYCRAYLPSEGVPA TDVAKRMKSEYKNCAECDTLVCLSEMRAHIRTCQKYIDKYG
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 3 |
Zinc finger 1 of the RING E3 ligase, RNF125, interacts with the E2 to enhance ubiquitylation. Middleton, A.J., Barzak, F.M., Fokkens, T.J. et al. Structure (2023) 31:1208-1219.e5. DOI 10.1016/j.str.2023.07.007 · PubMed
Other PDB entries of the same protein (UniProt P62837 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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