PDBe 2o25

X-ray diffraction
2.6Å resolution

Ubiquitin-Conjugating Enzyme E2-25 kDa Complexed With SUMO-1-Conjugating Enzyme UBC9

Released:
Source organism: Homo sapiens
Entry authors: Walker JR, Avvakumov GV, Xue S, Newman EM, Mackenzie F, Weigelt J, Sundstrom M, Arrowsmith CH, Edwards AM, Bochkarev A, Dhe-Paganon S, Structural Genomics Consortium (SGC)

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:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
SUMO-conjugating enzyme UBC9 Chains: C, D
Molecule details ›
Chains: C, D
Length: 160 amino acids
Theoretical weight: 18.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P63279 (Residues: 1-158; Coverage: 100%)
Gene names: UBC9, UBCE9, UBE2I
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme
Ubiquitin-conjugating enzyme E2 K Chains: A, B
Molecule details ›
Chains: A, B
Length: 202 amino acids
Theoretical weight: 22.57 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P61086 (Residues: 1-200; Coverage: 100%)
Gene names: HIP2, LIG, UBE2K
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P1
Unit cell:
a: 41.874Å b: 68.498Å c: 91.277Å
α: 85.05° β: 80.85° γ: 75.83°
R-values:
R R work R free
0.231 0.228 0.291
Expression system: Escherichia coli BL21(DE3)