MolNFT v1 · #7834 · protein
Structure of active conformations of GIA1 and the mechanism of GTP hydrolysis
1GIL · G protein gi alpha 1: “Structure of active conformations of GIA1 and the mechanism of GTP hydrolysis”. X-ray diffraction, 2 ligands (GSP, MG), 3 pockets (best druggability 0.73). MolNFT v1 #7834 on GenesisL1: 3D structure, binding…
- PDB
- 1GIL
- Type
- protein
- Length
- 310 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- G protein gi alpha 1
- UniProt
- P10824
- Ligands
- GSP, MG
- Pockets
- 3 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | G protein gi alpha 1 | protein | 310 | 52% helix, 15% strand | P10824 |
Ligands and binding sites
- GSP · 5'-guanosine-diphosphate-monothiophosphate · 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
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 308 | 0.73 | 0.86 | 43 | MG, GSP |
| 2 | 224 | 0.60 | 0.81 | 24 | empty |
| 3 | 83 | 0.35 | 0.75 | 16 | empty |
Compared structures
- 1GIL · Structure of active conformations of GIA1 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 0.99
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 1GIL · PDBe 1GIL · UniProt P10824
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