PDBe 3op0

X-ray diffraction
2.52Å resolution

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

Released:
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:
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. 
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

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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
UniProt:
  • Canonical: P00533 (Residues: 1066-1076; Coverage: 1%)
Gene names: EGFR, ERBB, ERBB1, HER1
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)
UniProt:
  • Canonical: Q9ULV8 (Residues: 9-323; Coverage: 67%)
Gene names: CBL3, CBLC, RNF57
Sequence domains:
Structure domains:

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-values:
R R work R free
0.255 0.214 0.266
Expression systems:
  • Not provided
  • Escherichia coli BL21(DE3)