› 6uuo

X-ray diffraction
3.29Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147199 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein kinase B-raf Chains: A, B
Molecule details ›
Chains: A, B
Length: 284 amino acids
Theoretical weight: 32.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P15056 (Residues: 444-723; Coverage: 37%)
Gene names: BRAF, BRAF1, RAFB1
Sequence domains: Protein tyrosine and serine/threonine kinase

Ligands and Environments

1 bound ligand:
Ligand QH1 2 x QH1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P212121
Unit cell:
a: 52.059Å b: 104.244Å c: 109.904Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.264 0.263 0.288
Expression system: Escherichia coli

Quick links

Citations

18 review citations

Trends in kinase drug discovery: targets, indications and inhibitor design.
Attwood et al. (2021)
17 more

2 mentions without citation

Functional characterization of a PROTAC directed against BRAF mutant V600E.
Posternak et al. (2020)
1 more