› 3ffa

X-ray diffraction
2.3Å resolution

Crystal Structure of a fast activating G protein mutant

Released:
DOI: 10.2210/pdb3ffa/pdb
PDB entry 3ffa coloured by chain, front view.
PDB entry 3ffa coloured by chain, side view.
PDB entry 3ffa coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Structural evidence for a sequential release mechanism for activation of heterotrimeric G proteins.
Kapoor N, Menon ST, Chauhan R, Sachdev P, Sakmar TP
J Mol Biol 393 882-97 (2009)
PMID: 19703466

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145470 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Guanine nucleotide-binding protein G(i) subunit alpha-1 Chain: A
Molecule details ›
Chain: A
Length: 360 amino acids
Theoretical weight: 40.95 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P10824 (Residues: 1-354; Coverage: 100%)
Gene names: Gnai-1, Gnai1
Sequence domains: G-protein alpha subunit
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand GSP 1 x GSP
Ligand MG 1 x MG
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P3221
Unit cell:
a: 79.008Å b: 79.008Å c: 105.667Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.185 0.252
Expression system: Escherichia coli

Quick links

Citations

6 review citations

pH sensing and regulation in cancer.
Damaghi et al. (2013)
5 more

1 mention without citation

Evaluating caveolin interactions: do proteins interact with the caveolin scaffolding domain through a widespread aromatic residue-rich motif?
Byrne et al. (2012)