Crystal structure of ubiquitin-conjugating enzyme E2-25kDa (Huntington interacting protein 2) M172A mutant. Determined by X-ray diffraction at 1.86 Å resolution. Released 26 Aug 2008.
Explore 3E46 in 3D Show helices and sheets RCSB PDB PDBe
3E46 contains 11 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 | 3-18 | 16 | |
| α-helix | 20-23 | 4 | |
| β-strand | 27-31 | 5 | 1 |
| β-strand | 38-44 | 7 | 1 |
| α-helix | 45-46 | 2 | |
| β-strand | 55-61 | 7 | 1 |
| α-helix | 70-71 | 2 | |
| β-strand | 72-75 | 4 | 1 |
| β-strand | 81 | 1 | 2 |
| β-strand | 84 | 1 | 2 |
| β-strand | 90 | 1 | 1 |
| β-strand | 91 | 1 | 2 |
| α-helix | 94-96 | 3 | |
| α-helix | 106-118 | 13 | |
| α-helix | 128-136 | 9 | |
| α-helix | 138-153 | 16 | |
| α-helix | 160-171 | 12 | |
| α-helix | 176-185 | 10 | |
| α-helix | 190-199 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin-conjugating enzyme E2-25 kDa | A | protein | 253 | Homo sapiens | P61086 (AlphaFold model) |
>3E46_1 Ubiquitin-conjugating enzyme E2-25 kDa (chains A) MHHHHHHSSGLVPRGSGMKETAAAKFERQHMDSPDLGTDDDDKAMADIGSEFDMANIAVQ RIKREFKEVLKSEETSKNQIKVDLVDENFTELRGEIAGPPDTPYEGGRYQLEIKIPETYP FNPPKVRFITKIWHPNISSVTGAICLDILKDQWAAAMTLRTVLLSLQALLAAAEPDDPQD AVVANQYKQNPEMFKQTARLWAHVYAGAPVSSPEYTKKIENLCAAGFDRNAVIVALSSKS WDVETATELLLSN
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 1 |
Structure of full-length ubiquitin-conjugating enzyme E2-25K (huntingtin-interacting protein 2). Wilson, R.C., Hughes, R.C., Flatt, J.W. et al. Acta Crystallogr Sect F Struct Biol Cryst Commun (2009) 65:440-444. DOI 10.1107/S1744309109011117 · PubMed
Other PDB entries of the same protein (UniProt P61086 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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