› 5c9c

X-ray diffraction
2.7Å 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

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-147194 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein kinase B-raf Chains: A, B
Molecule details ›
Chains: A, B
Length: 307 amino acids
Theoretical weight: 35.25 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P15056 (Residues: 432-726; Coverage: 39%)
Gene names: BRAF, BRAF1, RAFB1
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand 4Z5 2 x 4Z5
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P41212
Unit cell:
a: 93.88Å b: 93.88Å c: 165.55Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.194 0.238
Expression system: Trichoplusia ni

Quick links

Citations

65 review citations

KRAS: The Critical Driver and Therapeutic Target for Pancreatic Cancer.
Waters et al. (2018)
64 more

9 mentions without citation

Development of small-molecule therapeutics and strategies for targeting RAF kinase in BRAF-mutant colorectal cancer.
Pan et al. (2018)
8 more