› 2ckg

X-ray diffraction
2.45Å resolution

The structure of SENP1 SUMO-2 co-complex suggests a structural basis for discrimination between SUMO paralogues during processing

Released:
DOI: 10.2210/pdb2ckg/pdb
PDB entry 2ckg coloured by chain, front view.
PDB entry 2ckg coloured by chain, side view.
PDB entry 2ckg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing.
Shen LN, Dong C, Liu H, Naismith JH, Hay RT
Biochem J 397 279-88 (2006)
PMID: 16553580

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192807 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sentrin-specific protease 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 225 amino acids
Theoretical weight: 26.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9P0U3 (Residues: 419-644; Coverage: 35%)
Gene name: SENP1
Sequence domains: Ulp1 protease family, C-terminal catalytic domain
Structure domains: Adenoviral Proteinase; Chain A

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P3121
Unit cell:
a: 71.981Å b: 71.981Å c: 200.64Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.215 0.219 0.279
Expression system: Escherichia coli

Quick links

Citations

22 review citations

The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition.
Gareau et al. (2010)
21 more

4 mentions without citation

Advances in the development of SUMO specific protease (SENP) inhibitors.
Kumar et al. (2015)
3 more