PDBe 1k2p

X-ray diffraction
2.1Å resolution

Crystal structure of Bruton's tyrosine kinase domain

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein kinase BTK Chains: A, B
Molecule details ›
Chains: A, B
Length: 263 amino acids
Theoretical weight: 30.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q06187 (Residues: 397-659; Coverage: 40%)
Gene names: AGMX1, ATK, BPK, BTK
Sequence domains: Protein tyrosine kinase
Structure domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P212121
Unit cell:
a: 45Å b: 104Å c: 116Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.28 0.221 0.287
Expression system: Escherichia coli