PDBe 3op0

X-ray diffraction
2.52Å resolution

Crystal structure of Cbl-c (Cbl-3) TKB domain in complex with EGFR pY1069 peptide

Source organism: Homo sapiens
Entry authors: Chaikuad A, Guo K, Cooper CDO, Ayinampudi V, Krojer T, Ugochukwu E, Muniz JRC, Vollmar M, Canning P, von Delft F, Arrowsmith CH, Weigelt J, Edwards AM, Bountra C, Bullock A, Structural Genomics Consortium (SGC)

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:
  • not assigned

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase CBL-C Chains: A, B
Molecule details ›
Chains: A, B
Length: 323 amino acids
Theoretical weight: 36.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: NEW Q9ULV8 (Residues: 9-323; Coverage: 67%)
Gene names: CBL3, CBLC, RNF57
Sequence domains:
Structure domains:
Epidermal growth factor receptor Chains: C, D
Molecule details ›
Chains: C, D
Length: 11 amino acids
Theoretical weight: 1.28 KDa
Source organism: Homo sapiens
Expression system: Not provided
  • Canonical: NEW P00533 (Residues: 1066-1076; Coverage: 1%)
Gene names: EGFR, ERBB, ERBB1, HER1

Ligands and Environments

2 bound ligands:

3 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P65
Unit cell:
a: 90.25Å b: 90.25Å c: 191.581Å
α: 90° β: 90° γ: 120°
R R work R free
0.255 0.214 0.266
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided