TDP2 UBA Domain Bound to Ubiquitin at 0.85 Angstroms Resolution, Crystal Form 1. Determined by X-ray diffraction at 0.85 Å resolution. Released 29 Apr 2020.
Explore 6Q00 in 3D Show helices and sheets RCSB PDB PDBe
6Q00 contains 8 α-helices and 7 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 |
|---|---|---|---|
| β-strand | 2-7 | 6 | 1 |
| β-strand | 12-16 | 5 | 1 |
| β-strand | 22 | 1 | 2 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 41-45 | 5 | 1 |
| β-strand | 48-49 | 2 | 1 |
| β-strand | 55 | 1 | 2 |
| α-helix | 57-59 | 3 | |
| β-strand | 66-71 | 6 | 1 |
| α-helix | 72 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 23-36 | 14 | |
| α-helix | 40-49 | 10 | |
| α-helix | 54-62 | 9 | |
| α-helix | 64-65 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin | A | protein | 76 | Homo sapiens | P0CG48 (AlphaFold model) |
| Tyrosyl-DNA phosphodiesterase 2 | B | protein | 45 | Homo sapiens | O95551 (AlphaFold model) |
>6Q00_1 Ubiquitin (chains A) MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG
>6Q00_2 Tyrosyl-DNA phosphodiesterase 2 (chains B) SNARRLLCVEFASVASCDAAVAQCFLAENDWEMERALNSYFEPPV
Ubiquitin stimulated reversal of topoisomerase 2 DNA-protein crosslinks by TDP2. Schellenberg, M.J., Appel, C.D., Riccio, A.A. et al. Nucleic Acids Res (2020) 48:6310-6325. DOI 10.1093/nar/gkaa318 · PubMed
Other PDB entries of the same protein (UniProt P0CG48 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 6Q00 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.