› 5vr3

X-ray diffraction
2.1Å resolution

Crystal structure of the BRS domain of BRAF

Released:
DOI: 10.2210/pdb5vr3/pdb
PDB entry 5vr3 coloured by chain, front view.
PDB entry 5vr3 coloured by chain, side view.
PDB entry 5vr3 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
MEK drives BRAF activation through allosteric control of KSR proteins.
Lavoie H, Sahmi M, Maisonneuve P, Marullo SA, Thevakumaran N, Jin T, Kurinov I, Sicheri F, Therrien M
Nature 554 549-553 (2018)
PMID: 29433126

Function and Biology Details

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

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: 88 amino acids
Theoretical weight: 9.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P15056 (Residues: 36-114; Coverage: 10%)
Gene names: BRAF, BRAF1, RAFB1

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P3121
Unit cell:
a: 41.563Å b: 41.563Å c: 98.855Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.21 0.224
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

22 review citations

ERK signalling: a master regulator of cell behaviour, life and fate.
Lavoie et al. (2020)
21 more

2 mentions without citation

Ras isoform-specific expression, chromatin accessibility, and signaling.
Nussinov et al. (2021)
1 more