› 3q96

X-ray diffraction
3.1Å 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:
homo dimer
monomeric (preferred)
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: 282 amino acids
Theoretical weight: 32.15 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P15056 (Residues: 446-727; Coverage: 37%)
Gene names: BRAF, BRAF1, RAFB1
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 0NF 2 x 0NF
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: P41212
Unit cell:
a: 94.029Å b: 94.029Å c: 165.264Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.227 0.288
Expression system: Spodoptera frugiperda

Quick links

Citations

9 citation in other articles

BRAF Mutants Evade ERK-Dependent Feedback by Different Mechanisms that Determine Their Sensitivity to Pharmacologic Inhibition.
Yao et al. (2015)
8 more

2 mentions without citation

A spatial simulation approach to account for protein structure when identifying non-random somatic mutations.
Ryslik et al. (2014)
1 more