Crystal Structure of UbcH5B in Complex with the RING-U5BR Fragment of AO7. Determined by X-ray diffraction at 1.78 Å resolution. Released 28 Oct 2015.
Explore 5D1K in 3D Show helices and sheets RCSB PDB PDBe
5D1K contains 15 α-helices and 16 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 | 3-15 | 13 | |
| α-helix | 17-18 | 2 | |
| 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 | 71 | 1 | 2 |
| β-strand | 75 | 1 | 3 |
| β-strand | 78 | 1 | 3 |
| β-strand | 83 | 1 | 1 |
| β-strand | 84 | 1 | 3 |
| α-helix | 87-89 | 3 | |
| α-helix | 99-111 | 13 | |
| α-helix | 121-129 | 9 | |
| α-helix | 131-141 | 11 | |
| α-helix | 142-146 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 134 | 1 | 4 |
| β-strand | 141 | 1 | 4 |
| β-strand | 148-150 | 3 | 5 |
| β-strand | 156-158 | 3 | 5 |
| α-helix | 159-174 | 16 | |
| β-strand | 197 | 1 | 6 |
| α-helix | 203 | 1 | |
| β-strand | 204 | 1 | 6 |
| α-helix | 205-206 | 2 | |
| α-helix | 209-214 | 6 | |
| α-helix | 216-218 | 3 | |
| α-helix | 229-247 | 19 | |
| β-strand | 251 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin-conjugating enzyme E2 D2 | A | protein | 147 | Homo sapiens | P62837 (AlphaFold model) |
| E3 ubiquitin-protein ligase RNF25 | B | protein | 133 | Homo sapiens | Q96BH1 (AlphaFold model) |
>5D1K_1 Ubiquitin-conjugating enzyme E2 D2 (chains A) MALKRIHKELNDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDY PFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLV PEIARIYKTDREKYNRIAREWTQKYAM
>5D1K_2 E3 ubiquitin-protein ligase RNF25 (chains B) TDNNIPHGQCVICLYGFQEKEAFTKTPCYHYFHCHCLARYIQHMEQELKAQGQEQEQERQ HATTKQKAVGVQCPVCREPLVYDLASLKAAPEPQQPMELYQPSAESLRQQEERKRLYQRQ QERGGIIDLEAER
Water and common crystallization additives (PEG, EDO) are not listed.
Insights into Ubiquitination from the Unique Clamp-like Binding of the RING E3 AO7 to the E2 UbcH5B. Li, S., Liang, Y.H., Mariano, J. et al. J Biol Chem (2015) 290:30225-30239. DOI 10.1074/jbc.M115.685867 · 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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