PDBe 1b47

X-ray diffraction
2.2Å resolution

STRUCTURE OF THE N-TERMINAL DOMAIN OF CBL IN COMPLEX WITH ITS BINDING SITE IN ZAP-70

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:
Cellular component:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase CBL Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 304 amino acids
Theoretical weight: 35.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P22681 (Residues: 47-350; Coverage: 34%)
Gene names: CBL, CBL2, RNF55
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: C2
Unit cell:
a: 159.96Å b: 105.48Å c: 84.92Å
α: 90° β: 92.06° γ: 90°
R-values:
R R work R free
0.218 0.218 0.266
Expression system: Escherichia coli