2ooa

X-ray diffraction
1.56Å resolution

crystal structure of the UBA domain from Cbl-b ubiquitin ligase

Released:

Function and Biology Details

Reaction catalysed:
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-171596 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase CBL-B Chains: A, B
Molecule details ›
Chains: A, B
Length: 52 amino acids
Theoretical weight: 5.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q13191 (Residues: 924-973; Coverage: 5%)
Gene names: CBLB, Nbla00127, RNF56
Structure domains: DNA helicase RuvA subunit, C-terminal domain

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: C2221
Unit cell:
a: 46.138Å b: 50.199Å c: 78.343Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.204 0.24
Expression system: Escherichia coli BL21