› 1b47

X-ray diffraction
2.2Å resolution

STRUCTURE OF THE N-TERMINAL DOMAIN OF CBL IN COMPLEX WITH ITS BINDING SITE IN ZAP-70

Released:
DOI: 10.2210/pdb1b47/pdb
PDB entry 1b47 coloured by chain, front view.
PDB entry 1b47 coloured by chain, side view.
PDB entry 1b47 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase.
Meng W, Sawasdikosol S, Burakoff SJ, Eck MJ
Nature 398 84-90 (1999)
PMID: 10078535

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 domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149771 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase CBL Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 304 amino acids
Theoretical weight: 35.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P22681 (Residues: 47-350; Coverage: 34%)
Gene names: CBL, CBL2, RNF55
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CA 3 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: C2
Unit cell:
a: 159.96Å b: 105.48Å c: 84.92Å
α: 90° β: 92.06° γ: 90°
R-values:
R R work R free
0.218 0.218 0.266
Expression system: Escherichia coli

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Citations

48 review citations

Signaling--2000 and beyond.
Hunter T. (2000)
47 more

5 mentions without citation

Massive peptide sharing between viral and human proteomes.
Kanduc et al. (2008)
4 more