Research workbench
Structure of the K180P mutant of gi alpha subunit bound to ALF4 and GDP
Analyse Structure of the K180P mutant of gi alpha 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
- 1SVK
- 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(I), alpha-1 subunit
- EC
- 3.6.1.46
- UniProt
- P10824
- Ligands
- ALF, GDP, MG
- Pockets
- 3 · best druggability 0.75
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(I), alpha-1 subunit (EC 3.6.1.46) | 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
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 | 164 | 0.75 | 0.92 | 31 | MG, ALF, GDP |
| 2 | 282 | 0.61 | 0.80 | 35 | empty |
| 3 | 67 | 0.29 | 0.73 | 11 | empty |
Compared structures
- 1SVK · Structure of the K180P mutant of Gi alpha 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 1SVK · PDBe 1SVK · UniProt P10824
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