Research workbench
GPCR-beta arrestin structure in lipid bilayer
Analyse GPCR-beta arrestin structure in lipid bilayer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6U1N
- Type
- protein
- Length
- 864 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Muscarinic acetylcholine receptor M2, vasopressin V2 receptor chimera; Beta-arrestin-1…
- UniProt
- P08172, P30518, P29066, V9HW68, Q7Z3Y4
- Ligands
- 2CU
- Pockets
- 12 · best druggability 0.82
Structure
electron microscopy · 4 distinct chains · 28% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| R | Muscarinic acetylcholine receptor M2, vasopressin V2 receptor chimera | protein | 278 | 77% helix, 1% strand | P08172, P30518 |
| C | Beta-arrestin-1 | protein | 359 | 4% helix, 45% strand | P29066 |
| H | FAB30 heavy chain | protein | 119 | 10% helix, 49% strand | V9HW68 |
| L | FAB30 light chain | protein | 108 | 3% helix, 46% strand | Q7Z3Y4 |
Ligands and binding sites
- 2CU · 3-amino-5-chloro-N-cyclopropyl-4-methyl-6-[2-(4-methylpiperazin-1-yl)-2-oxoethoxy]thieno[2,3-b]pyridine-2-carboxamide · ligand · chains R
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 892 | 0.82 | 0.84 | 114 | empty |
| 2 | 811 | 0.80 | 0.83 | 88 | 2CU |
| 3 | 940 | 0.78 | 0.80 | 74 | empty |
| 4 | 53 | 0.67 | 0.95 | 21 | empty |
| 5 | 120 | 0.53 | 0.82 | 27 | empty |
Interfaces
5 interfaces between chains.
- R–C · 1315 Ų buried · 34 hydrogen bonds · protein-protein
- H–L · 735 Ų buried · 3 hydrogen bonds · protein-protein
- C–H · 695 Ų buried · 9 hydrogen bonds · protein-protein
- C–L · 178 Ų buried · 3 hydrogen bonds · protein-protein
- R–L · 94 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified, 4 disulfide (phosphorylation, disulfide).
Compared structures
- 6U1N · GPCR-Beta arrestin structure in lipid bilayer · the same entry in another collection · chain R against R, TM-score 1.00
- P29066 · AlphaFold monomer V2.0 prediction for beta-arrestin-1 (P29066) · a predicted model of the same protein · chain C against A, TM-score 0.89
- P08172 · AlphaFold monomer V2.0 prediction for muscarinic acetylcholine receptor M2 (P08172) · a predicted model of the same protein · chain R against A, TM-score 0.86
- P30518 · AlphaFold monomer V2.0 prediction for vasopressin V2 receptor (P30518) · a predicted model of the same protein · chain R against A, TM-score 0.78
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 P08172
- Every structure of UniProt P30518
- Every structure of UniProt P29066
- Every structure of UniProt V9HW68
- Every structure of UniProt Q7Z3Y4
- Elsewhere: RCSB PDB 6U1N · PDBe 6U1N · UniProt P08172 · UniProt P30518 · UniProt P29066 · UniProt V9HW68 · UniProt Q7Z3Y4
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.