PDBe 5v1a

X-ray diffraction
2.14Å resolution

Structure of S. cerevisiae Ulp2:Csm1 complex

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of the alpha-linked peptide bond in the sequence Gly-Gly-|-Ala-Thr-Tyr at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptide, Smt3, leading to the mature form of the protein. A second reaction involves the cleavage of an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin-like-specific protease 2 Chain: B
Molecule details ›
Chain: B
Length: 26 amino acids
Theoretical weight: 2.89 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P40537 (Residues: 821-845; Coverage: 2%)
Gene names: SMT4, ULP2, YIL031W
Monopolin complex subunit CSM1 Chain: A
Molecule details ›
Chain: A
Length: 122 amino acids
Theoretical weight: 14.14 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P25651 (Residues: 69-190; Coverage: 64%)
Gene names: CSM1, SPO86, YCR086W, YCR86W
Sequence domains: Chromosome segregation protein Csm1/Pcs1

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL14-1
Spacegroup: P43212
Unit cell:
a: 46.737Å b: 46.737Å c: 124.638Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.239 0.234 0.278
Expression system: Escherichia coli