PDBe 5dfl

X-ray diffraction
2.1Å resolution

Crystal structure of Ube2K~Ubiquitin conjugate

Released:
Source organism: Homo sapiens
Primary publication:
The molecular basis of lysine 48 ubiquitin chain synthesis by Ube2K.
OpenAccess logo Sci Rep 5 16793 (2015)
PMID: 26592444

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 Chain: B
Molecule details ›
Chain: B
Length: 76 amino acids
Theoretical weight: 8.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG47 (Residues: 153-228; Coverage: 33%)
Gene name: UBB
Sequence domains: Ubiquitin family
Ubiquitin-conjugating enzyme E2 K Chain: A
Molecule details ›
Chain: A
Length: 200 amino acids
Theoretical weight: 22.41 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:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: C2
Unit cell:
a: 146.324Å b: 37.557Å c: 61.001Å
α: 90° β: 90.43° γ: 90°
R-values:
R R work R free
0.197 0.195 0.235
Expression system: Escherichia coli