› 5eql

X-ray diffraction
2.49Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158458 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
SUMO-Affirmer-S2D5 Chain: A
Molecule details ›
Chain: A
Length: 116 amino acids
Theoretical weight: 13.25 KDa
Source organism: synthetic construct
Expression system: Escherichia coli BL21(DE3)
Structure domains: Nuclear Transport Factor 2; Chain: A,
Small ubiquitin-related modifier 2 Chain: B
Molecule details ›
Chain: B
Length: 77 amino acids
Theoretical weight: 8.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P61956 (Residues: 14-89; Coverage: 80%)
Gene names: SMT3B, SMT3H2, SUMO2
Sequence domains: Ubiquitin-2 like Rad60 SUMO-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P3121
Unit cell:
a: 74.27Å b: 74.27Å c: 59.717Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.22 0.218 0.243
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Visualizing ubiquitination in mammalian cells.
van Wijk et al. (2019)
5 more

2 mentions without citation

Generation of specific inhibitors of SUMO-1- and SUMO-2/3-mediated protein-protein interactions using Affimer (Adhiron) technology.
Hughes et al. (2017)
1 more