PDBe 3pfv

X-ray diffraction
2.27Å resolution

Crystal structure of Cbl-b 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, Muniz JRC, Vollmar M, Canning P, Gileadi O, 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:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase CBL-B Chains: A, B
Molecule details ›
Chains: A, B
Length: 315 amino acids
Theoretical weight: 36.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q13191 (Residues: 38-344; Coverage: 31%)
Gene names: CBLB, Nbla00127, RNF56
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
UniProt:
  • Canonical: P00533 (Residues: 1066-1076; Coverage: 1%)
Gene names: EGFR, ERBB, ERBB1, HER1

Ligands and Environments


1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P21
Unit cell:
a: 60.063Å b: 98.934Å c: 61.978Å
α: 90° β: 110.63° γ: 90°
R-values:
R R work R free
0.219 0.216 0.262
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided