MolNFT v1 · #167749 · protein
Structure of G-alpha-Q bound to its chaperone ric-8A
6VU5 · Resistance to inhibitors of cholinesterase-8A (ric-8A): “Structure of G-alpha-Q bound to its chaperone ric-8A”. Electron microscopy, 7 pockets (best druggability 0.60). MolNFT v1 #167749 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6VU5
- Type
- protein
- Length
- 603 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Resistance to inhibitors of cholinesterase-8A (ric-8A); Guanine nucleotide-binding…
- UniProt
- P50148
- Pockets
- 7 · best druggability 0.60
Structure
electron microscopy · 2 distinct chains · 46% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Resistance to inhibitors of cholinesterase-8A (ric-8A) | protein | 468 | 49% helix, 1% strand | — |
| B | Guanine nucleotide-binding protein G(Q) subunit alpha | protein | 135 | 33% helix, 8% strand | P50148 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 353 | 0.60 | 0.77 | 40 | empty |
| 2 | 166 | 0.54 | 0.80 | 31 | empty |
| 3 | 93 | 0.43 | 0.78 | 23 | empty |
| 4 | 76 | 0.42 | 0.80 | 23 | empty |
| 5 | 118 | 0.37 | 0.73 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 2636 Ų buried · 25 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 6VU5 · Structure of G-alpha-q bound to its chaperone Ric-8A · the same entry in another collection · chain A against A, TM-score 1.00
- P50148 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(Q) subunit… · a predicted model of the same protein · chain B against A, TM-score 0.71
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 P50148
- Elsewhere: RCSB PDB 6VU5 · PDBe 6VU5 · UniProt P50148
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