› 1git

X-ray diffraction
2.6Å resolution

STRUCTURE OF GTP-BINDING PROTEIN

Released:
DOI: 10.2210/pdb1git/pdb
PDB entry 1git coloured by chain, front view.
PDB entry 1git coloured by chain, side view.
PDB entry 1git coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Structure of the GDP-Pi complex of Gly203-->Ala gialpha1: a mimic of the ternary product complex of galpha-catalyzed GTP hydrolysis.
Berghuis AM, Lee E, Raw AS, Gilman AG, Sprang SR
Structure 4 1277-90 (1996)
PMID: 8939752

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure 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: 353 amino acids
Theoretical weight: 40.28 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P10824 (Residues: 2-354; Coverage: 100%)
Gene names: Gnai-1, Gnai1
Sequence domains: G-protein alpha subunit
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand PO4 1 x PO4
Ligand GDP 1 x GDP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F2
Spacegroup: P43212
Unit cell:
a: 77.1Å b: 77.1Å c: 144.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.186 0.279
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Physiological regulation of G protein-linked signaling.
Morris et al. (1999)
9 more

8 mentions without citation

Invited review: Activation of G proteins by GTP and the mechanism of Gα-catalyzed GTP hydrolysis.
Sprang SR. (2016)
7 more