PDBe 3k9o

X-ray diffraction
1.8Å resolution

The crystal structure of E2-25K and UBB+1 complex

Released:
Source organism: Homo sapiens
Entry authors: Kang GB, Ko S, Song SM, Lee W, Eom SH

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):
Ubiquitin-conjugating enzyme E2 K Chain: A
Molecule details ›
Chain: A
Length: 201 amino acids
Theoretical weight: 22.49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P61086 (Residues: 1-200; Coverage: 100%)
Gene names: HIP2, LIG, UBE2K
Sequence domains:
Structure domains:
Ubiquitin Chain: B
Molecule details ›
Chain: B
Length: 96 amino acids
Theoretical weight: 10.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG48 (Residues: 608-683; Coverage: 11%)
Gene name: UBC
Sequence domains: Ubiquitin family
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: PAL/PLS BEAMLINE 4A
Spacegroup: C2
Unit cell:
a: 102.48Å b: 50.547Å c: 71.323Å
α: 90° β: 125.01° γ: 90°
R-values:
R R work R free
0.206 0.187 0.233
Expression system: Escherichia coli