MolNFT v1 · #100535 · protein
Crystal structure of the K345L variant of the gi ALPHA1 subunit bound to GDP
4N0E · Guanine nucleotide-binding protein G(I) subunit alpha-1: “Crystal structure of the K345L variant of the gi ALPHA1 subunit bound to GDP”. X-ray diffraction, 2 ligands (GDP, SO4), 3 pockets (best druggability 0.70). MolNFT v1 #100535…
- PDB
- 4N0E
- Type
- protein
- Length
- 330 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
- EC
- 3.6.5.1
- UniProt
- P10824
- Ligands
- GDP, SO4
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Guanine nucleotide-binding protein G(I) subunit alpha-1 (EC 3.6.5.1) | protein | 330 | 51% helix, 13% strand | P10824 |
Ligands and binding sites
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 | 153 | 0.70 | 0.90 | 29 | GDP |
| 2 | 245 | 0.58 | 0.79 | 31 | empty |
| 3 | 58 | 0.31 | 0.76 | 11 | empty |
Compared structures
- 4N0E · Crystal structure of the K345L variant of the Gi alpha1 subunit bound to 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 0.92
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 4N0E · PDBe 4N0E · UniProt P10824
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