5ELU: SUMO-Affirmer-S2B3

Isoform-specific inhibition of SUMO-dependent protein-protein interactions. Determined by X-ray diffraction at 2.35 Å resolution. Released 16 Nov 2016.

Method
X-ray diffraction
Resolution
2.35 Å
Organisms
synthetic construct, Homo sapiens
Chains
2
Atoms
1,461
Mol. weight
22.76 kDa
Released
16 Nov 2016

Explore 5ELU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5ELU contains 3 α-helices and 9 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, 4 β-strands

ElementResiduesLengthSheet
α-helix35-5218
β-strand57-69131
β-strand76-87121
β-strand90-100111
α-helix105-1073
β-strand113-12081
Chain B: 1 helix, 5 β-strands
ElementResiduesLengthSheet
β-strand17-2481
β-strand29-3571
α-helix41-5111
β-strand58-6251
β-strand65-6621
β-strand83-8861

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
SUMO-Affirmer-S2B3Aprotein118synthetic construct
Small ubiquitin-related modifier 2Bprotein77Homo sapiensP61956 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5ELU_1 SUMO-Affirmer-S2B3 (chains A)
MASAATGVRAVPGNENSLEIEELARFAVDEHNKKENALLEFVRVVKAKEQVDLTRFPVTT
MYYLTLEAKDGGKKKLYEAKVWVKGYLLEELKHNFKELQEFKPVGDAAAAHHHHHHHH
Sequence of entity 2 (B), FASTA
>5ELU_2 Small ubiquitin-related modifier 2 (chains B)
MNNDHINLKVAGQDGSVVQFKIKRHTPLSKLMKAYCERQGLSMRQIRFRFDGQPINETDT
PAQLEMEDEDTIDVFQQ

Primary citation

Generation of specific inhibitors of SUMO-1- and SUMO-2/3-mediated protein-protein interactions using Affimer (Adhiron) technology. Hughes, D.J., Tiede, C., Penswick, N. et al. Sci Signal (2017) 10. DOI 10.1126/scisignal.aaj2005 · PubMed

Other PDB entries of the same protein (UniProt P61956 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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