5hky

X-ray diffraction
1.8Å resolution

Crystal structure of c-Cbl TKBD domain in complex with SPRY2 peptide (36-60, pY55) Refined to 1.8A Resolution (P6 form)

Released:
Source organism: Homo sapiens
Entry authors: Lovell S, Battaile KP, Mehzabeen N, Zhang N, Cooper A, Gao P, Perez RP

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:
Biological process:
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 Chain: A
Molecule details ›
Chain: A
Length: 308 amino acids
Theoretical weight: 35.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P22681 (Residues: 47-351; Coverage: 34%)
Gene names: CBL, CBL2, RNF55
Sequence domains:
Structure domains:
Protein sprouty homolog 2 Chain: B
Molecule details ›
Chain: B
Length: 26 amino acids
Theoretical weight: 2.99 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: O43597 (Residues: 35-60; Coverage: 8%)
Gene name: SPRY2

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P6
Unit cell:
a: 122.81Å b: 122.81Å c: 58.44Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.158 0.157 0.18
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided