PDBe 1yvh

X-ray diffraction
2.05Å resolution

Crystal Structure of the c-Cbl TKB Domain in Complex with the APS pTyr-618 Phosphopeptide

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: A
Molecule details ›
Chain: A
Length: 329 amino acids
Theoretical weight: 38.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P22681 (Residues: 23-23, 25-351; Coverage: 36%)
Gene names: CBL, CBL2, RNF55
Sequence domains:
Structure domains:
SH2B adapter protein 2 Chain: B
Molecule details ›
Chain: B
Length: 13 amino acids
Theoretical weight: 1.64 KDa
Source organism: Rattus norvegicus
Expression system: Not provided
UniProt:
  • Canonical: Q9Z200 (Residues: 609-621; Coverage: 2%)
Gene names: Aps, Sh2b2

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P6
Unit cell:
a: 122.257Å b: 122.257Å c: 55.131Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.209 0.209 0.247
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided