Human Ubiquitin-Conjugating Enzyme (E2) UbcH5b mutant Ile37Ala. Determined by X-ray diffraction at 1.5 Å resolution. Released 6 Dec 2005.
Explore 2ESO in 3D Show helices and sheets RCSB PDB PDBe
2ESO contains 7 α-helices and 8 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 | 0-15 | 16 | |
| 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 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin-conjugating enzyme E2 D2 | A | protein | 149 | Homo sapiens | P62837 (AlphaFold model) |
>2ESO_1 Ubiquitin-conjugating enzyme E2 D2 (chains A) GAMALKRIHKELNDLARDPPAQCSAGPVGDDMFHWQATAMGPNDSPYQGGVFFLTIHFPT DYPFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDP LVPEIARIYKTDREKYNRIAREWTQKYAM
Mechanistic insight into the allosteric activation of a ubiquitin-conjugating enzyme by RING-type ubiquitin ligases. Ozkan, E., Yu, H., Deisenhofer, J. Proc Natl Acad Sci U S A (2005) 102:18890-18895. DOI 10.1073/pnas.0509418102 · 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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