5vyk

X-ray diffraction
1.75Å resolution

Crystal structure of the BRS domain of BRAF in complex with the CC-SAM domain of KSR1

Released:

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:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kinase suppressor of Ras 1; Serine/threonine-protein kinase B-raf Chains: A, C
Molecule details ›
Chains: A, C
Length: 232 amino acids
Theoretical weight: 25.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P15056 (Residues: 36-110; Coverage: 10%)
  • Canonical: Q8IVT5 (Residues: 27-172; Coverage: 16%)
Gene names: BRAF, BRAF1, KSR, KSR1, RAFB1
Sequence domains: SAM like domain present in kinase suppressor RAS 1

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: C2
Unit cell:
a: 179.796Å b: 54.336Å c: 51.864Å
α: 90° β: 106.68° γ: 90°
R-values:
R R work R free
0.218 0.217 0.239
Expression system: Escherichia coli