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A conserved phenylalanine as relay between the 5 helix and the GDP binding region of heterotrimeric G protein
Analyse A conserved phenylalanine as relay between the 5 helix and the GDP binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PAQ
- Type
- protein
- Length
- 316 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Guanine nucleotide-binding protein G(I) subunit alpha-1
- UniProt
- P10824
- Ligands
- GSP, MG
- Pockets
- 4 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Guanine nucleotide-binding protein G(I) subunit alpha-1 | protein | 316 | 53% 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
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 198 | 0.77 | 0.92 | 31 | GSP, MG |
| 2 | 215 | 0.56 | 0.79 | 28 | empty |
| 3 | 70 | 0.32 | 0.74 | 17 | empty |
| 4 | 53 | 0.27 | 0.74 | 13 | empty |
Compared structures
- 4PAQ · A conserved phenylalanine as relay between the 5 helix and the GDP binding region of… · 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 4PAQ · PDBe 4PAQ · UniProt P10824
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