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Structures of active conformations of gi alpha 1 and the mechanism of GTP hydrolysis

Analyse Structures of active conformations of gi alpha 1 and the mechanism of GTP… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1GFI
Type
protein
Length
313 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Guanine nucleotide-binding protein G
UniProt
P10824
Ligands
ALF, GDP, MG
Pockets
2 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGuanine nucleotide-binding protein Gprotein31351% helix, 15% strandP10824

Ligands and binding sites

  • ALF · Tetrafluoroaluminate ion · ligand · chains A
  • GDP · Guanosine-5'-diphosphate · ligand · chains A
  • MG · Magnesium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12760.700.8544MG, ALF, GDP
23270.630.7933empty

Compared structures

  • 1GFI · Structures of active conformations of gi alpha 1 and the mechanism of GTP hydrolysis · the same entry in another collection · chain A against A, TM-score 1.00
  • P10824 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(I) subunit… · a predicted model of the same protein · chain A against A, TM-score 0.98

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