PDBe 5lnb

X-ray diffraction
2.3Å resolution

Crystal structure of the de-sumoylating protease

Released:
Entry authors: Eckhoff J, Dohmen J, Pichlo C, Baumann U

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:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin-like-specific protease 2 Chain: B
Molecule details ›
Chain: B
Length: 310 amino acids
Theoretical weight: 36.61 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P40537 (Residues: 411-710; Coverage: 29%)
Gene names: SMT4, ULP2, YIL031W
Sequence domains: Ulp1 protease family, C-terminal catalytic domain

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P212121
Unit cell:
a: 42.54Å b: 55.58Å c: 172.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.157 0.197
Expression system: Escherichia coli