Research workbench
Structure of the K349P mutant of gi alpha 1 subunit bound to ALF4 and GDP
Analyse Structure of the K349P mutant of gi alpha 1 subunit bound to ALF4 and GDP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZJY
- Type
- protein
- Length
- 317 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Guanine nucleotide-binding protein G(I), alpha-1 subunit
- EC
- 3.6.5.1
- UniProt
- P10824
- Ligands
- ALF, GDP, MG
- Pockets
- 3 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Guanine nucleotide-binding protein G(I), alpha-1 subunit (EC 3.6.5.1) | protein | 317 | 50% 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
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 | 208 | 0.72 | 0.88 | 37 | ALF, MG, GDP |
| 2 | 254 | 0.60 | 0.80 | 28 | empty |
| 3 | 96 | 0.36 | 0.75 | 20 | empty |
Compared structures
- 2ZJY · Structure of the K349P mutant of Gi alpha 1 subunit bound to ALF4 and GDP · 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 2ZJY · PDBe 2ZJY · UniProt P10824
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