› 5p9m

X-ray diffraction
1.41Å 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: 279 amino acids
Theoretical weight: 32.33 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q06187 (Residues: 382-659; Coverage: 42%)
Gene names: AGMX1, ATK, BPK, BTK
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand 7GB 1 x 7GB
Ligand DMS 1 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21212
Unit cell:
a: 70.958Å b: 104.377Å c: 38.107Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.179 0.2
Expression system: Trichoplusia ni

Quick links

Citations

18 review citations

The Src module: an ancient scaffold in the evolution of cytoplasmic tyrosine kinases.
Shah et al. (2018)
17 more

3 mentions without citation

Btk Inhibitors: A Medicinal Chemistry and Drug Delivery Perspective.
Brullo et al. (2021)
2 more