Research workbench
A galpha-I1 P-loop mutation prevents transition to the activated state
Analyse A galpha-I1 P-loop mutation prevents transition to the activated state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QE0
- Type
- protein
- Length
- 944 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Guanine nucleotide-binding protein G(I) subunit alpha-1; KB752 peptide
- EC
- 3.6.5.1
- UniProt
- P63096
- Ligands
- GDP, MG
- Pockets
- 9 · best druggability 0.76
Structure
x-ray diffraction · 5 distinct chains · 50% helix, 14% 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 | 314 | 50% helix, 14% strand | P63096 |
| B | Guanine nucleotide-binding protein G(I) subunit alpha-1 (EC 3.6.5.1) | protein | 314 | 50% helix, 15% strand | P63096 |
| C | Guanine nucleotide-binding protein G(I) subunit alpha-1 (EC 3.6.5.1) | protein | 299 | 50% helix, 13% strand | P63096 |
| G | KB752 peptide | protein | 11 | 36% helix, 9% strand | — |
| F | KB752 peptide | protein | 6 | 67% helix, 0% strand | — |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · 3 copies · chains A, B, C
- MG · Magnesium ion · metal · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 445 | 0.76 | 0.85 | 50 | MG, GDP |
| 2 | 478 | 0.72 | 0.82 | 58 | MG, GDP |
| 3 | 459 | 0.72 | 0.82 | 60 | MG, GDP |
| 4 | 365 | 0.61 | 0.78 | 45 | empty |
| 5 | 221 | 0.59 | 0.80 | 27 | empty |
Interfaces
5 interfaces between chains.
- B–G · 733 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 617 Ų buried · 5 hydrogen bonds · protein-protein
- A–F · 476 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 286 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 41 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3QE0 · A Galpha-i1 P-loop mutation prevents transition to the activated state · the same entry in another collection · chain F against F, TM-score 1.00
- P63096 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(I) subunit… · a predicted model of the same protein · chain C 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 P63096
- Elsewhere: RCSB PDB 3QE0 · PDBe 3QE0 · UniProt P63096
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