PDBe 3vrr

X-ray diffraction
2Å resolution

Crystal structure of the tyrosine kinase binding domain of Cbl-c (PL mutant) in complex with phospho-EGFR peptide

Released:

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

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase CBL-C Chain: A
Molecule details ›
Chain: A
Length: 331 amino acids
Theoretical weight: 36.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9ULV8 (Residues: 1-323; Coverage: 68%)
Gene names: CBL3, CBLC, RNF57
Sequence domains:
Structure domains:
Epidermal growth factor receptor Chain: C
Molecule details ›
Chain: C
Length: 13 amino acids
Theoretical weight: 1.63 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P00533 (Residues: 1062-1074; Coverage: 1%)
Gene names: EGFR, ERBB, ERBB1, HER1

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: C2221
Unit cell:
a: 93.24Å b: 108.683Å c: 54.677Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.186 0.234
Expression systems:
  • Escherichia coli
  • Not provided