› 3i2d

X-ray diffraction
2.6Å resolution

Crystal Structure of S. Cerevisiae SUMO E3 Ligase SIZ1

Released:
DOI: 10.2210/pdb3i2d/pdb
PDB entry 3i2d coloured by chain, front view.
PDB entry 3i2d coloured by chain, side view.
PDB entry 3i2d coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNA.
Yunus AA, Lima CD
Mol Cell 35 669-82 (2009)
PMID: 19748360

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170002 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 SUMO-protein ligase SIZ1 Chain: A
Molecule details ›
Chain: A
Length: 371 amino acids
Theoretical weight: 41.7 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q04195 (Residues: 112-465; Coverage: 39%)
Gene names: SIZ1, ULL1, YDR409W
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P212121
Unit cell:
a: 44.487Å b: 88.98Å c: 105.598Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.211 0.259
Expression system: Escherichia coli

Quick links

Citations

18 review citations

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

3 mentions without citation

Emerging roles of sumoylation in the regulation of actin, microtubules, intermediate filaments, and septins.
Alonso et al. (2015)
2 more