6yyk

X-ray diffraction
2.04Å resolution

Crystal Structure of 1,5-dimethylindoline-2,3-dione covalently bound to the PH domain of Bruton's tyrosine kinase mutant R28C

Released:
Source organism: Homo sapiens
Entry authors: Brear P, Wagstaff J, Hyvonen M

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (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: 19.93 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:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P21
Unit cell:
a: 48.199Å b: 60.344Å c: 58.058Å
α: 90° β: 96.57° γ: 90°
R-values:
R R work R free
0.231 0.228 0.296
Expression system: Escherichia coli BL21(DE3)