› 5np2

X-ray diffraction
1.6Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132602 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein kinase ABL1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 61 amino acids
Theoretical weight: 6.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00519 (Residues: 64-120; Coverage: 5%)
Gene names: ABL, ABL1, JTK7
Sequence domains: SH3 domain
Structure domains: SH3 Domains

Ligands and Environments

No bound ligands
1 modified residue:
Ligand PTR 4 x PTR

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Spacegroup: C2221
Unit cell:
a: 48.63Å b: 83.18Å c: 57.87Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.189 0.222
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Novel Roles of SH2 and SH3 Domains in Lipid Binding.
Sipeki et al. (2021)
5 other articles

1 mention without citation

Structural insights into the tyrosine phosphorylation-mediated inhibition of SH3 domain-ligand interactions.
Merő et al. (2019)