› 6htf

X-ray diffraction
2.1Å 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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-166833 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tyrosine-protein kinase BTK Chain: A
Molecule details ›
Chain: A
Length: 117 amino acids
Theoretical weight: 13.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q06187 (Residues: 271-383; Coverage: 17%)
Gene names: AGMX1, ATK, BPK, BTK
Sequence domains: SH2 domain
rF10 repebody Chain: B
Molecule details ›
Chain: B
Length: 274 amino acids
Theoretical weight: 31.1 KDa
Source organism: synthetic construct
Expression system: Escherichia coli

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P21212
Unit cell:
a: 145.521Å b: 32.947Å c: 80.624Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.21 0.256
Expression systems:
  • Escherichia coli BL21
  • Escherichia coli

Quick links

Citations

7 review citations

Bleeding by Bruton Tyrosine Kinase-Inhibitors: Dependency on Drug Type and Disease.
von Hundelshausen et al. (2021)
6 more

1 mention without citation

Btk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms.
Duarte et al. (2020)