PDBe 3ob1

X-ray diffraction
2.2Å resolution

Crystal structure of c-Cbl TKB domain in complex with double phosphorylated Spry2 peptide

Released:

Function and Biology Details

Reaction 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. 
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 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:
Protein sprouty homolog 2 Chain: A
Molecule details ›
Chain: A
Length: 12 amino acids
Theoretical weight: 1.56 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: O43597 (Residues: 49-60; Coverage: 4%)
Gene name: SPRY2

Ligands and Environments

No bound ligands

2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER PROTEUM X8
Spacegroup: P6
Unit cell:
a: 122.092Å b: 122.092Å c: 55.689Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.183 0.181 0.223
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided