› 5elj

X-ray diffraction
1.98Å resolution

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159009 (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 1 Chain: B
Molecule details ›
Chain: B
Length: 83 amino acids
Theoretical weight: 9.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P63165 (Residues: 18-97; Coverage: 79%)
Gene names: OK/SW-cl.43, SMT3C, SMT3H3, SUMO1, UBL1
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 I04
Spacegroup: P212121
Unit cell:
a: 36.23Å b: 70.72Å c: 83.63Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.188 0.236
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

Affimer proteins are versatile and renewable affinity reagents.
Tiede et al. (2017)
1 more