6au6

X-ray diffraction
1.7Å resolution

Crystal structure of GDP-bound human GNAS R201C mutant

Released:
Source organism: Homo sapiens
Primary publication:
Disease-Causing Mutations in the G Protein Gαs Subvert the Roles of GDP and GTP.
Cell 173 1254-1264.e11 (2018)
PMID: 29628140

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-158950 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Guanine nucleotide-binding protein G(s) subunit alpha isoforms short Chain: A
Molecule details ›
Chain: A
Length: 377 amino acids
Theoretical weight: 44.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P63092 (Residues: 7-394; Coverage: 95%)
Gene names: GNAS, GNAS1, GSP
Sequence domains: G-protein alpha subunit
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P212121
Unit cell:
a: 37.37Å b: 85.58Å c: 125.64Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.168 0.2
Expression system: Escherichia coli