› 1rfa

Solution NMR

NMR SOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN OF C-RAF-1

Released:
DOI: 10.2210/pdb1rfa/pdb
PDB entry 1rfa coloured by chain, ensemble of 30 models, front view.
PDB entry 1rfa coloured by chain, ensemble of 30 models, side view.
PDB entry 1rfa coloured by chain, ensemble of 30 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of the Ras-binding domain of c-Raf-1 and identification of its Ras interaction surface.
Emerson SD, Madison VS, Palermo RE, Waugh DS, Scheffler JE, Tsao KL, Kiefer SE, Liu SP, Fry DC
Biochemistry 34 6911-8 (1995)
PMID: 7766599

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137335 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RAF proto-oncogene serine/threonine-protein kinase Chain: A
Molecule details ›
Chain: A
Length: 79 amino acids
Theoretical weight: 8.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04049 (Residues: 54-132; 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Escherichia coli

Quick links

Citations

14 review citations

G protein mechanisms: insights from structural analysis.
Sprang SR. (1997)
13 more

8 mentions without citation

What lessons can be learned from studying the folding of homologous proteins?
Nickson et al. (2010)
7 more