Research workbench
Structure of G-alpha-I bound to its chaperone ric-8A
Analyse Structure of G-alpha-I bound to its chaperone ric-8A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VU8
- Type
- protein
- Length
- 669 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Resistance to inhibitors of cholinesterase 8 homolog a (C. elegans); Guanine…
- UniProt
- B1H241, P63096
- Pockets
- 13 · best druggability 0.76
Structure
electron microscopy · 2 distinct chains · 47% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Resistance to inhibitors of cholinesterase 8 homolog a (C. elegans) | protein | 485 | 53% helix, 0% strand | B1H241 |
| B | Guanine nucleotide-binding protein G(I) subunit alpha-1 | protein | 184 | 32% helix, 10% strand | P63096 |
Pockets
13 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 679 | 0.76 | 0.82 | 77 | empty |
| 2 | 480 | 0.74 | 0.83 | 57 | empty |
| 3 | 135 | 0.66 | 0.88 | 32 | empty |
| 4 | 243 | 0.65 | 0.83 | 42 | empty |
| 5 | 107 | 0.63 | 0.88 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 3020 Ų buried · 24 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 6VU8 · Structure of G-alpha-i bound to its chaperone Ric-8A · the same entry in another collection · chain A against A, 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 B against A, TM-score 0.72
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 B1H241
- Every structure of UniProt P63096
- Elsewhere: RCSB PDB 6VU8 · PDBe 6VU8 · UniProt B1H241 · UniProt P63096
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