› 4y95

X-ray diffraction
1.6Å resolution

Crystal structure of the kinase domain of Bruton's tyrosine kinase with mutations in the activation loop

Released:
DOI: 10.2210/pdb4y95/pdb
PDB entry 4y95 coloured by chain, front view.
PDB entry 4y95 coloured by chain, side view.
PDB entry 4y95 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 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 266 amino acids
Theoretical weight: 31.04 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q3ZC95 (Residues: 395-659; Coverage: 40%)
Gene name: BTK
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand 746 4 x 746
Ligand GOL 8 x GOL
Ligand BME 3 x BME
Ligand PE4 2 x PE4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P1
Unit cell:
a: 50.929Å b: 79.067Å c: 79.178Å
α: 90.73° β: 89.9° γ: 89.99°
R-values:
R R work R free
0.155 0.155 0.184
Expression system: Escherichia coli

Quick links

Citations

16 review citations

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

1 mention without citation

Autoinhibition of Bruton's tyrosine kinase (Btk) and activation by soluble inositol hexakisphosphate.
Wang et al. (2015)