1wm3

X-ray diffraction
1.2Å resolution

Crystal structure of human SUMO-2 protein

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Small ubiquitin-related modifier 2 Chain: A
Molecule details ›
Chain: A
Length: 72 amino acids
Theoretical weight: 8.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P61956 (Residues: 17-88; Coverage: 76%)
Gene names: SMT3B, SMT3H2, SUMO2
Sequence domains: Ubiquitin-2 like Rad60 SUMO-like
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL17B2
Spacegroup: R3
Unit cell:
a: 74.964Å b: 74.964Å c: 33.231Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.124 0.119 0.185
Expression system: Escherichia coli BL21(DE3)