Structure of SdeA DUB Domain disulfide crosslinked with Ubiquitin. Determined by X-ray diffraction at 2.81 Å resolution. Released 20 Sept 2023.
Explore 8EFW in 3D Show helices and sheets RCSB PDB PDBe
8EFW contains 16 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 | 5-7 | 3 | |
| β-strand | 10-11 | 2 | 1 |
| α-helix | 12-22 | 11 | |
| α-helix | 27-29 | 3 | |
| β-strand | 30-33 | 4 | 2 |
| β-strand | 36-38 | 3 | 2 |
| α-helix | 41-47 | 7 | |
| β-strand | 49-56 | 8 | 2 |
| β-strand | 62-63 | 2 | 1 |
| β-strand | 64-70 | 7 | 2 |
| β-strand | 75-79 | 5 | 2 |
| α-helix | 84-95 | 12 | |
| α-helix | 99 | 1 | |
| β-strand | 103-106 | 4 | 2 |
| α-helix | 109-110 | 2 | |
| α-helix | 120-121 | 2 | |
| α-helix | 122-126 | 5 | |
| α-helix | 127-133 | 7 | |
| α-helix | 138-140 | 3 | |
| α-helix | 141-154 | 14 | |
| α-helix | 158-169 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-7 | 6 | 3 |
| β-strand | 12-16 | 5 | 3 |
| β-strand | 22 | 1 | 4 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 41-44 | 4 | 3 |
| β-strand | 49 | 1 | 3 |
| α-helix | 50-51 | 2 | |
| β-strand | 55 | 1 | 4 |
| β-strand | 66-71 | 6 | 3 |
| β-strand | 74-75 | 2 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| SdeA | B | protein | 200 | Legionella pneumophila | Q5ZTK4 (AlphaFold model) |
| Ubiquitin | C | protein | 76 | Homo sapiens | P0CG47 (AlphaFold model) |
>8EFW_1 SdeA (chains B) PLGSMPKYVEGVELTQEGMHAIFARMGYGDITSGSIYNGVPTIDTGALNRQGFMPVLTGV GPHRDSGHWIMLIKGPGNQYYLFDPLGKTSGEGYQNILAAQLPMGSTLSVIPNGSGLNMG LCGYWVASAGLRAHQALNQHNPPTLLNVGQTITNEMRNELDHDGYRKITGWLRAVADEFP EGEPQLDGKALRENTEKDLK
>8EFW_2 Ubiquitin (chains C) MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGC
Cocrystallization of ubiquitin-deubiquitinase complexes through disulfide linkage. Negron Teron, K.I., Das, C. Acta Crystallogr D Struct Biol (2023) 79:1044-1055. DOI 10.1107/S2059798323008501 · PubMed
Other PDB entries of the same protein (UniProt Q5ZTK4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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