› 3vrn

X-ray diffraction
1.64Å resolution

Crystal structure of the tyrosine kinase binding domain of Cbl-c

Released:
DOI: 10.2210/pdb3vrn/pdb
PDB entry 3vrn coloured by chain, front view.
PDB entry 3vrn coloured by chain, side view.
PDB entry 3vrn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural flexibility regulates phosphopeptide-binding activity of the tyrosine kinase binding domain of Cbl-c.
Takeshita K, Tezuka T, Isozaki Y, Yamashita E, Suzuki M, Kim M, Yamanashi Y, Yamamoto T, Nakagawa A
J Biochem 152 487-95 (2012)
PMID: 22888118

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193938 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase CBL-C Chain: A
Molecule details ›
Chain: A
Length: 331 amino acids
Theoretical weight: 36.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9ULV8 (Residues: 1-323; Coverage: 68%)
Gene names: CBL3, CBLC, RNF57
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: C2221
Unit cell:
a: 93.223Å b: 107.617Å c: 54.773Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.182 0.218
Expression system: Escherichia coli

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Citations

3 citation in other articles

High-yield cell-free synthesis of human EGFR by IRES-mediated protein translation in a continuous exchange cell-free reaction format.
Quast et al. (2016)
2 more