› 3k54

X-ray diffraction
1.94Å resolution

Structures of human Bruton's tyrosine kinase in active and inactive conformations suggests a mechanism of activation for TEC family kinases.

Released:
DOI: 10.2210/pdb3k54/pdb
PDB entry 3k54 coloured by chain, front view.
PDB entry 3k54 coloured by chain, side view.
PDB entry 3k54 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of human Bruton's tyrosine kinase in active and inactive conformations suggest a mechanism of activation for TEC family kinases.
Marcotte DJ, Liu YT, Arduini RM, Hession CA, Miatkowski K, Wildes CP, Cullen PF, Hong V, Hopkins BT, Mertsching E, Jenkins TJ, Romanowski MJ, Baker DP, Silvian LF
Protein Sci 19 429-39 (2010)
PMID: 20052711

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-170299 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein kinase BTK Chain: A
Molecule details ›
Chain: A
Length: 283 amino acids
Theoretical weight: 32.65 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q06187 (Residues: 382-659; Coverage: 42%)
Gene names: AGMX1, ATK, BPK, BTK
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 1N1 1 x 1N1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: P21212
Unit cell:
a: 73.438Å b: 104.622Å c: 38.107Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.199 0.258
Expression system: Spodoptera frugiperda

Quick links

Citations

16 review citations

FDA-approved small-molecule kinase inhibitors.
Wu et al. (2015)
15 more

17 mentions without citation

Bruton's Tyrosine Kinase Targeting in Multiple Myeloma.
Von Suskil et al. (2021)
16 more