PDBe 1qly

Solution NMR

NMR STUDY OF THE SH3 DOMAIN FROM BRUTON'S TYROSINE KINASE, 20 STRUCTURES

Released:

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein kinase BTK Chain: A
Molecule details ›
Chain: A
Length: 58 amino acids
Theoretical weight: 6.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q06187 (Residues: 216-273; Coverage: 9%)
Gene names: AGMX1, ATK, BPK, BTK
Sequence domains: SH3 domain
Structure domains: SH3 Domains

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: SIMULATED ANNEALING
Expression system: Escherichia coli BL21