PDBe 2bf8

X-ray diffraction
2.3Å resolution

Crystal structure of SUMO modified ubiquitin conjugating enzyme E2- 25K

Released:

Function and Biology Details

Reaction catalysed:
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin-conjugating enzyme E2 K Chain: A
Molecule details ›
Chain: A
Length: 159 amino acids
Theoretical weight: 17.85 KDa
Source organism: Bos taurus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: NEW P61085 (Residues: 1-155; Coverage: 78%)
Gene names: HIP2, UBE2K
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme
Small ubiquitin-related modifier 1 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: NEW P63165 (Residues: 21-97; Coverage: 76%)
Gene names: OK/SW-cl.43, SMT3C, SMT3H3, SUMO1, UBL1
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: ESRF BEAMLINE ID14-4
Spacegroup: P43212
Unit cell:
a: 58.391Å b: 58.391Å c: 162.842Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.21 0.279
Expression system: Escherichia coli BL21(DE3)