6UYZ: K46-acetylated SUMO1

Crystal structure of K46-acetylated SUMO1 in complex with phosphorylated DAXX. Determined by X-ray diffraction at 1.4 Å resolution. Released 27 Nov 2019.

Method
X-ray diffraction
Resolution
1.4 Å
Organism
Homo sapiens
Chains
4
Atoms
1,774
Mol. weight
23.14 kDa
Released
27 Nov 2019

Explore 6UYZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6UYZ contains 11 α-helices and 12 β-strands across 4 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: 5 helices, 5 β-strands

ElementResiduesLengthSheet
β-strand21-2771
β-strand33-3971
α-helix45-5511
α-helix59-613
β-strand62-6651
β-strand69-7021
α-helix71-722
α-helix77-804
β-strand87-9261
α-helix93-942
Chains B and D: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand11-1331
Chain C: 6 helices, 5 β-strands
ElementResiduesLengthSheet
α-helix18-203
β-strand21-2772
β-strand33-3972
α-helix45-5511
α-helix59-613
β-strand62-6652
β-strand69-7022
α-helix71-722
α-helix77-804
β-strand87-9262
α-helix93-942

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Small ubiquitin-related modifier 1A, Cprotein83Homo sapiensP63165 (AlphaFold model)
phosphorylated DAXXB, Dprotein17Homo sapiens
Sequence of entity 1 (A, C), FASTA
>6UYZ_1 Small ubiquitin-related modifier 1 (chains A, C)
GSKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYAQRQGVPMNSLRFLFEGQRIADN
HTPKELGMEEEDVIEVYQEQTGG
Sequence of entity 2 (B, D), FASTA
>6UYZ_2 phosphorylated DAXX (chains B, D)
GSGEAEERIIVLSDSDY

Primary citation

Acetylation of SUMO1 Alters Interactions with the SIMs of PML and Daxx in a Protein-Specific Manner. Mascle, X.H., Gagnon, C., Wahba, H.M. et al. Structure (2020) 28:157-168.e5. DOI 10.1016/j.str.2019.11.019 · PubMed

Other PDB entries of the same protein (UniProt P63165 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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