› 2z0p

X-ray diffraction
2.58Å resolution

Crystal structure of PH domain of Bruton's tyrosine kinase

Released:
DOI: 10.2210/pdb2z0p/pdb
PDB entry 2z0p coloured by chain, front view.
PDB entry 2z0p coloured by chain, side view.
PDB entry 2z0p coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the Bruton's tyrosine kinase PH domain with phosphatidylinositol.
Murayama K, Kato-Murayama M, Mishima C, Akasaka R, Shirouzu M, Fukui Y, Yokoyama S
Biochem Biophys Res Commun 377 23-8 (2008)
PMID: 18809383

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-170299 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein kinase BTK Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 169 amino acids
Theoretical weight: 19.98 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q06187 (Residues: 2-170; Coverage: 26%)
Gene names: AGMX1, ATK, BPK, BTK
Sequence domains:
Structure domains: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

Ligands and Environments

2 bound ligands:
Ligand ZN 4 x ZN
Ligand 4PT 4 x 4PT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P21
Unit cell:
a: 59.417Å b: 62.499Å c: 117.064Å
α: 90° β: 94.33° γ: 90°
R-values:
R R work R free
0.242 0.242 0.3
Expression system: Spodoptera frugiperda

Quick links

Citations

5 review citations

Bruton's tyrosine kinase (Btk): function, regulation, and transformation with special emphasis on the PH domain.
Mohamed et al. (2009)
4 more

6 mentions without citation

Lipid and Protein Co-Regulation of PI3K Effectors Akt and Itk in Lymphocytes.
Wang et al. (2015)
5 more