MolNFT v1 · #7731 · protein
Structures of active conformations of gi alpha 1 and the mechanism of GTP hydrolysis
1GFI · Guanine nucleotide-binding protein G: “Structures of active conformations of gi alpha 1 and the mechanism of GTP hydrolysis”. X-ray diffraction, 3 ligands (ALF, GDP, MG), 2 pockets (best druggability 0.70). MolNFT v1 #7731 on…
- 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).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Guanine nucleotide-binding protein G | protein | 313 | 51% helix, 15% strand | P10824 |
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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 276 | 0.70 | 0.85 | 44 | MG, ALF, GDP |
| 2 | 327 | 0.63 | 0.79 | 33 | empty |
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
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P10824
- Elsewhere: RCSB PDB 1GFI · PDBe 1GFI · UniProt P10824
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