MolNFT v1 · #181809 · protein
Full length ALPHA1 glycine receptor in presence of 1MM glycine and 32UM tetrahydrocannabinol state 1
7M6Q · Glycine receptor subunit ALPHAZ1: “Full length ALPHA1 glycine receptor in presence of 1MM glycine and 32UM tetrahydrocannabinol state 1”. Electron microscopy, 3 ligands (GLY, TCI, NAG), 20 pockets (best druggability 0.79). MolNFT v1…
- PDB
- 7M6Q
- Type
- protein
- Length
- 1,795 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycine receptor subunit ALPHAZ1
- UniProt
- O93430
- Ligands
- GLY, TCI, NAG
- Pockets
- 20 · best druggability 0.79
Structure
electron microscopy · 1 distinct chain · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Glycine receptor subunit ALPHAZ1 | protein | 359 | 37% helix, 25% strand | O93430 |
Ligands and binding sites
- GLY · Glycine · ligand · 5 copies · chains A, B, E, C, D
- TCI · (6aR,10aR)-6,6,9-trimethyl-3-pentyl-6a,7,8,10a-tetrahydro-6H-benzo[c]chromen-1-ol · ligand · 5 copies · chains A, B, C, D, E
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A, B, C, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 627 | 0.79 | 0.84 | 49 | empty |
| 2 | 460 | 0.70 | 0.81 | 53 | empty |
| 3 | 356 | 0.69 | 0.82 | 48 | empty |
| 4 | 596 | 0.68 | 0.78 | 60 | empty |
| 5 | 558 | 0.67 | 0.77 | 56 | empty |
Interfaces
5 interfaces between chains.
- A–B · 2348 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 2293 Ų buried · 13 hydrogen bonds · protein-protein
- A–E · 2281 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 2249 Ų buried · 13 hydrogen bonds · protein-protein
- D–E · 2243 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide, 5 glycan (disulfide, N-glycosylation).
Compared structures
- 7M6Q · Full length alpha1 Glycine receptor in presence of 1mM Glycine and 32uM… · the same entry in another collection · chain E against E, TM-score 1.00
- O93430 · AlphaFold monomer V2.0 prediction for glycine receptor subunit ALPHAZ1 (O93430) · a predicted model of the same protein · chain B against A, TM-score 0.96
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 O93430
- Elsewhere: RCSB PDB 7M6Q · PDBe 7M6Q · UniProt O93430
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