2KQS: Small ubiquitin-related modifier 1

Phosphorylation of SUMO-interacting motif by CK2 enhances Daxx SUMO binding activity. Determined by solution NMR. Released 1 Dec 2010.

Method
Solution NMR
Organism
Homo sapiens
Chains
2
Atoms
928
Mol. weight
13.59 kDa
Released
1 Dec 2010

Explore 2KQS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 2 helices, 7 β-strands

ElementResiduesLengthSheet
β-strand1511
β-strand1911
β-strand22-2762
β-strand33-3862
α-helix44-5512
β-strand62-6652
β-strand69-7022
α-helix77-804
β-strand86-9272
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix736-7383

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Small ubiquitin-related modifier 1Aprotein99Homo sapiensP63165 (AlphaFold model)
Death domain-associated protein 6Bprotein22Homo sapiensQ9UER7 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2KQS_1 Small ubiquitin-related modifier 1 (chains A)
GSMSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVP
MNSLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQTGG
Sequence of entity 2 (B), FASTA
>2KQS_2 Death domain-associated protein 6 (chains B)
GSKTSVATQCDPEEIIVLSDSD

Primary citation

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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