› 5csx

X-ray diffraction
2.51Å 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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147194 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein kinase B-raf Chain: A
Molecule details ›
Chain: A
Length: 282 amino acids
Theoretical weight: 32.03 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P15056 (Residues: 442-721; Coverage: 37%)
Gene names: BRAF, BRAF1, RAFB1
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand 54J 1 x 54J
Ligand GLC 1 x GLC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: C2221
Unit cell:
a: 49.375Å b: 116.136Å c: 102.423Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.217 0.282
Expression system: Escherichia coli

Quick links

Citations

15 review citations

New perspectives for targeting RAF kinase in human cancer.
Karoulia et al. (2017)
14 more

6 mentions without citation

Challenges and Opportunities in the Crusade of BRAF Inhibitors: From 2002 to 2022.
Singh et al. (2023)
5 more