1k1f

X-ray diffraction
2.2Å resolution

Structure of the Bcr-Abl Oncoprotein Oligomerization domain

Released:
Source organism: Homo sapiens
Primary publication:
Structure of the Bcr-Abl oncoprotein oligomerization domain.
Nat Struct Biol 9 117-20 (2002)
PMID: 11780146

Function and Biology Details

Reaction catalysed:
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-145740 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Breakpoint cluster region protein Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 72 amino acids
Theoretical weight: 8.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11274 (Residues: 1-72; Coverage: 6%)
Gene names: BCR, BCR1, D22S11
Sequence domains: Bcr-Abl oncoprotein oligomerisation domain
Structure domains: Bcr-Abl oncoprotein oligomerisation domain

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P21
Unit cell:
a: 35.988Å b: 121.173Å c: 60.432Å
α: 90° β: 93.03° γ: 90°
R-values:
R R work R free
0.27 0.262 0.295
Expression system: Escherichia coli