› 4y93

X-ray diffraction
1.7Å resolution

Crystal structure of the PH-TH-kinase construct of Bruton's tyrosine kinase (Btk)

Released:
DOI: 10.2210/pdb4y93/pdb
PDB entry 4y93 coloured by chain, front view.
PDB entry 4y93 coloured by chain, side view.
PDB entry 4y93 coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Autoinhibition of Bruton's tyrosine kinase (Btk) and activation by soluble inositol hexakisphosphate.
Wang Q, Vogan EM, Nocka LM, Rosen CE, Zorn JA, Harrison SC, Kuriyan J
Elife 4 (2015)
PMID: 25699547

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-174901 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein kinase Chain: A
Molecule details ›
Chain: A
Length: 446 amino acids
Theoretical weight: 51.89 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q3ZC95 (Residues: 1-168, 384-658; Coverage: 67%)
Gene name: BTK
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand ZN 1 x ZN
Ligand 746 1 x 746
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Unit cell:
a: 38.328Å b: 78.647Å c: 157.569Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.158 0.157 0.195
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Molecular Mechanisms of Human Disease Mediated by Oncogenic and Primary Immunodeficiency Mutations in Class IA Phosphoinositide 3-Kinases.
Dornan et al. (2018)
13 more

6 mentions without citation

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