2hl8

X-ray diffraction
2Å resolution

SUMO protease Ulp1 with the catalytic cysteine oxidized to a sulfinic acid

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:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-169739 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin-like-specific protease 1 Chain: A
Molecule details ›
Chain: A
Length: 221 amino acids
Theoretical weight: 25.68 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q02724 (Residues: 403-621; Coverage: 35%)
Gene names: LPB11C, ULP1, YPL020C
Sequence domains: Ulp1 protease family, C-terminal catalytic domain
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2
Unit cell:
a: 104.936Å b: 40.189Å c: 55.371Å
α: 90° β: 112° γ: 90°
R-values:
R R work R free
0.194 0.192 0.234
Expression system: Escherichia coli BL21