› 3ob2

X-ray diffraction
2.1Å resolution

Crystal structure of c-Cbl TKB domain in complex with double phosphorylated EGFR peptide

Released:
DOI: 10.2210/pdb3ob2/pdb
PDB entry 3ob2 coloured by chain, front view.
PDB entry 3ob2 coloured by chain, side view.
PDB entry 3ob2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Additional serine/threonine phosphorylation reduces binding affinity but preserves interface topography of substrate proteins to the c-Cbl TKB domain.
Sun Q, Jackson RA, Ng C, Guy GR, Sivaraman J
PLoS One 5 e12819 (2010)
PMID: 20877636

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:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132677 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Epidermal growth factor receptor Chain: A
Molecule details ›
Chain: A
Length: 12 amino acids
Theoretical weight: 1.58 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P00533 (Residues: 1063-1074; Coverage: 1%)
Gene names: EGFR, ERBB, ERBB1, HER1
E3 ubiquitin-protein ligase CBL Chain: B
Molecule details ›
Chain: B
Length: 329 amino acids
Theoretical weight: 38.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P22681 (Residues: 25-351; Coverage: 36%)
Gene names: CBL, CBL2, RNF55
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
2 modified residues:
Ligand PTR 1 x PTR
Ligand SEP 1 x SEP

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER PROTEUM X8
Spacegroup: P6
Unit cell:
a: 122.771Å b: 122.771Å c: 55.425Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.184 0.183 0.217
Expression systems:
  • Not provided
  • Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Degrons in cancer.
Mészáros et al. (2017)
1 more

2 mentions without citation

Accuracy and precision of protein structures determined by magic angle spinning NMR spectroscopy: for some 'with a little help from a friend'.
Russell et al. (2019)
1 more