PDBe 2oo9

X-ray diffraction
2.1Å resolution

crystal structure of the UBA domain from human c-Cbl 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. 
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase CBL Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 46 amino acids
Theoretical weight: 5.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P22681 (Residues: 856-895; Coverage: 4%)
Gene names: CBL, CBL2, RNF55
Sequence domains: UBA/TS-N domain
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: CHESS BEAMLINE F2
Spacegroup: P41212
Unit cell:
a: 82.025Å b: 82.025Å c: 56.194Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.216 0.26
Expression system: Escherichia coli BL21