› 1bwn

X-ray diffraction
2.1Å resolution

PH DOMAIN AND BTK MOTIF FROM BRUTON'S TYROSINE KINASE MUTANT E41K IN COMPLEX WITH INS(1,3,4,5)P4

Released:
DOI: 10.2210/pdb1bwn/pdb
PDB entry 1bwn coloured by chain, front view.
PDB entry 1bwn coloured by chain, side view.
PDB entry 1bwn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the PH domain from Bruton's tyrosine kinase in complex with inositol 1,3,4,5-tetrakisphosphate.
Baraldi E, Djinovic Carugo K, Hyvönen M, Surdo PL, Riley AM, Potter BV, O'Brien R, Ladbury JE, Saraste M
Structure 7 449-60 (1999)
PMID: 10196129

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

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170302 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein kinase BTK Chains: A, B
Molecule details ›
Chains: A, B
Length: 169 amino acids
Theoretical weight: 19.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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 2 x ZN
Ligand 4IP 4 x 4IP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: I4122
Unit cell:
a: 110.784Å b: 110.784Å c: 215.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.214 0.29
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

38 review citations

Synthesis and function of 3-phosphorylated inositol lipids.
Vanhaesebroeck et al. (2001)
37 more

8 mentions without citation

The role of hydrophobic interactions in positioning of peripheral proteins in membranes.
Lomize et al. (2007)
7 more