› 7n5y

X-ray diffraction
1.85Å resolution

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170299 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein kinase BTK Chain: A
Molecule details ›
Chain: A
Length: 283 amino acids
Theoretical weight: 32.69 KDa
Source organism: Homo sapiens
Expression system: unidentified baculovirus
UniProt:
  • Canonical: Q06187 (Residues: 382-659; Coverage: 42%)
Gene names: AGMX1, ATK, BPK, BTK
Sequence domains: Protein tyrosine and serine/threonine kinase

Ligands and Environments

3 bound ligands:
Ligand IMD 1 x IMD
Ligand 0CI 1 x 0CI
Ligand DMS 1 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: P21212
Unit cell:
a: 72.717Å b: 104.729Å c: 38.05Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.163 0.202
Expression system: unidentified baculovirus

Quick links

Citations

1 review citation

The Development of BTK Inhibitors: A Five-Year Update.
Tasso et al. (2021)

1 mention without citation

Structural Complementarity of Bruton's Tyrosine Kinase and Its Inhibitors for Implication in B-Cell Malignancies and Autoimmune Diseases.
Najmi et al. (2023)