› 1k2p

X-ray diffraction
2.1Å resolution

Crystal structure of Bruton's tyrosine kinase domain

Released:
DOI: 10.2210/pdb1k2p/pdb
PDB entry 1k2p coloured by chain, front view.
PDB entry 1k2p coloured by chain, side view.
PDB entry 1k2p coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of Bruton's tyrosine kinase domain suggests a novel pathway for activation and provides insights into the molecular basis of X-linked agammaglobulinemia.
Mao C, Zhou M, Uckun FM
J Biol Chem 276 41435-43 (2001)
PMID: 11527964

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 domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170301 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein kinase BTK Chains: A, B
Molecule details ›
Chains: A, B
Length: 263 amino acids
Theoretical weight: 30.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q06187 (Residues: 397-659; Coverage: 40%)
Gene names: AGMX1, ATK, BPK, BTK
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P212121
Unit cell:
a: 45Å b: 104Å c: 116Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.28 0.221 0.287
Expression system: Escherichia coli

Quick links

Citations

16 review citations

Regulation of protein kinases; controlling activity through activation segment conformation.
Nolen et al. (2004)
15 more

19 mentions without citation

The role of Bruton's tyrosine kinase in autoimmunity and implications for therapy.
Crofford et al. (2016)
18 more