Phosphorylation of SUMO-interacting motif by CK2 enhances Daxx SUMO binding activity. Determined by solution NMR. Released 1 Dec 2010.
Explore 2KQS in 3D Show helices and sheets RCSB PDB PDBe
2KQS contains 3 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 | 15 | 1 | 1 |
| β-strand | 19 | 1 | 1 |
| β-strand | 22-27 | 6 | 2 |
| β-strand | 33-38 | 6 | 2 |
| α-helix | 44-55 | 12 | |
| β-strand | 62-66 | 5 | 2 |
| β-strand | 69-70 | 2 | 2 |
| α-helix | 77-80 | 4 | |
| β-strand | 86-92 | 7 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 736-738 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Small ubiquitin-related modifier 1 | A | protein | 99 | Homo sapiens | P63165 (AlphaFold model) |
| Death domain-associated protein 6 | B | protein | 22 | Homo sapiens | Q9UER7 (AlphaFold model) |
>2KQS_1 Small ubiquitin-related modifier 1 (chains A) GSMSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVP MNSLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQTGG
>2KQS_2 Death domain-associated protein 6 (chains B) GSKTSVATQCDPEEIIVLSDSD
Structural and functional roles of Daxx SIM phosphorylation in SUMO paralog-selective binding and apoptosis modulation. Chang, C.C., Naik, M.T., Huang, Y.S. et al. Mol Cell (2011) 42:62-74. DOI 10.1016/j.molcel.2011.02.022 · PubMed
Other PDB entries of the same protein (UniProt P63165 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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