Structure of S. cerevisiae Ulp2:Csm1 complex. Determined by X-ray diffraction at 2.14 Å resolution. Released 17 May 2017.
Explore 5V1A in 3D Show helices and sheets RCSB PDB PDBe
5V1A contains 6 α-helices and 5 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 |
|---|---|---|---|
| α-helix | 71-82 | 12 | |
| β-strand | 84-91 | 8 | 1 |
| β-strand | 96-102 | 7 | 1 |
| β-strand | 116-123 | 8 | 1 |
| β-strand | 131-136 | 6 | 1 |
| α-helix | 143-152 | 10 | |
| α-helix | 155-158 | 4 | |
| β-strand | 161-164 | 4 | 1 |
| α-helix | 165-167 | 3 | |
| α-helix | 168-179 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 832-839 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin-like-specific protease 2 | B | protein | 26 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P40537 (AlphaFold model) |
| Monopolin complex subunit CSM1 | A | protein | 122 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P25651 (AlphaFold model) |
>5V1A_1 Ubiquitin-like-specific protease 2 (chains B) AEFTSPYFGRPSLKTRAKQFEGVSSP
>5V1A_2 Monopolin complex subunit CSM1 (chains A) ENSEVIKDLYEYLCNVRVHKSYEDDSGLWFDISQGTHSGGSSDDYSIMDYKLGFVKGQAQ VTEVIYAPVLKQRSTEELYSLQSKLPEYLFETLSFPLSSLNQFYNKIAKSLNKKREKKDE TE
Recruitment of a SUMO isopeptidase to rDNA stabilizes silencing complexes by opposing SUMO targeted ubiquitin ligase activity. Liang, J., Singh, N., Carlson, C.R. et al. Genes Dev (2017) 31:802-815. DOI 10.1101/gad.296145.117 · PubMed
Other PDB entries of the same protein (UniProt P40537 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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