PDBe 3buw

X-ray diffraction
1.45Å resolution

Crystal structure of c-Cbl-TKB domain complexed with its binding motif in Syk


Function and Biology Details

Reactions 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. 
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. 
Biochemical function:
Cellular component:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase CBL Chains: B, D
Molecule details ›
Chains: B, D
Length: 329 amino acids
Theoretical weight: 38.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P22681 (Residues: 23-351; Coverage: 36%)
Gene names: CBL, CBL2, RNF55
Sequence domains:
Structure domains:
Tyrosine-protein kinase SYK Chains: A, C
Molecule details ›
Chains: A, C
Length: 13 amino acids
Theoretical weight: 1.54 KDa
Source organism: Homo sapiens
Expression system: Not provided
  • Canonical: P43405 (Residues: 317-329; Coverage: 2%)
Gene name: SYK

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P21
Unit cell:
a: 63.793Å b: 104.809Å c: 52.778Å
α: 90° β: 89.83° γ: 90°
R R work R free
0.224 0.224 0.238
Expression systems:
  • Escherichia coli
  • Not provided