5V1A: S. cerevisiae Ulp2:Csm1 complex

Structure of S. cerevisiae Ulp2:Csm1 complex. Determined by X-ray diffraction at 2.14 Å resolution. Released 17 May 2017.

Method
X-ray diffraction
Resolution
2.14 Å
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Chains
2
Atoms
1,019
Mol. weight
17.03 kDa
Released
17 May 2017

Explore 5V1A in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 5 helices, 5 β-strands

ElementResiduesLengthSheet
α-helix71-8212
β-strand84-9181
β-strand96-10271
β-strand116-12381
β-strand131-13661
α-helix143-15210
α-helix155-1584
β-strand161-16441
α-helix165-1673
α-helix168-17912
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix832-8398

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ubiquitin-like-specific protease 2Bprotein26Saccharomyces cerevisiae (strain ATCC 204508 / S288c)P40537 (AlphaFold model)
Monopolin complex subunit CSM1Aprotein122Saccharomyces cerevisiae (strain ATCC 204508 / S288c)P25651 (AlphaFold model)
Sequence of entity 1 (B), FASTA
>5V1A_1 Ubiquitin-like-specific protease 2 (chains B)
AEFTSPYFGRPSLKTRAKQFEGVSSP
Sequence of entity 2 (A), FASTA
>5V1A_2 Monopolin complex subunit CSM1 (chains A)
ENSEVIKDLYEYLCNVRVHKSYEDDSGLWFDISQGTHSGGSSDDYSIMDYKLGFVKGQAQ
VTEVIYAPVLKQRSTEELYSLQSKLPEYLFETLSFPLSSLNQFYNKIAKSLNKKREKKDE
TE

Primary citation

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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