6UYO: K37-acetylated SUMO1

Crystal structure of K37-acetylated SUMO1 in complex with PML-SIM. Determined by X-ray diffraction at 1.64 Å resolution. Released 27 Nov 2019.

Method
X-ray diffraction
Resolution
1.64 Å
Organism
Homo sapiens
Chains
4
Atoms
1,571
Mol. weight
25.09 kDa
Released
27 Nov 2019

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

Secondary structure: helices and β-sheets

6UYO contains 9 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.

Chains A and C: 4 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
Chain B: 1 helix, 1 β-strand
ElementResiduesLengthSheet
β-strand11-1331
α-helix14-152
Chain D: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand11-1332

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Small ubiquitin-related modifier 1A, Cprotein83Homo sapiensP63165 (AlphaFold model)
Protein PMLB, Dprotein29Homo sapiensP29590 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>6UYO_1 Small ubiquitin-related modifier 1 (chains A, C)
GSKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYAQRQGVPMNSLRFLFEGQRIADN
HTPKELGMEEEDVIEVYQEQTGG
Sequence of entity 2 (B, D), FASTA
>6UYO_2 Protein PML (chains B, D)
GSGAGEAEERVVVISSSEDSDAENSSSRY

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:

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