1wm2

X-ray diffraction
1.6Å 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: 78 amino acids
Theoretical weight: 9.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P61956 (Residues: 12-89; Coverage: 82%)
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: RIGAKU MICROMAX-002
Spacegroup: R3
Unit cell:
a: 75.25Å b: 75.25Å c: 29.17Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.173 0.169 0.19
Expression system: Escherichia coli BL21(DE3)