PDBe 1c1y

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE OF RAP.GMPPNP IN COMPLEX WITH THE RAS-BINDING-DOMAIN OF C-RAF1 KINASE (RAFRBD).

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ras-related protein Rap-1A Chain: A
Molecule details ›
Chain: A
Length: 167 amino acids
Theoretical weight: 19.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62834 (Residues: 1-167; Coverage: 91%)
Gene names: KREV1, RAP1A
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
RAF proto-oncogene serine/threonine-protein kinase Chain: B
Molecule details ›
Chain: B
Length: 77 amino acids
Theoretical weight: 8.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04049 (Residues: 55-131; Coverage: 12%)
Gene names: RAF, RAF1
Sequence domains: Raf-like Ras-binding domain
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P212121
Unit cell:
a: 44.17Å b: 71.88Å c: 100.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.229 0.229 0.257
Expression system: Escherichia coli