MolNFT v1 · #85930 · protein
Mus musculus acetylcholinesterase in complex with (R)-C5685 at 2.5 a resolution.
4ARA: “Mus musculus acetylcholinesterase in complex with (R)-C5685 at 2.5 a resolution.”. X-ray diffraction, 3 ligands (C56, NAG, CL), 15 pockets (best druggability 0.78). MolNFT v1 #85930 on GenesisL1: 3D structure, binding sites and…
- PDB
- 4ARA
- Type
- protein
- Length
- 1,068 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylcholinesterase
- EC
- 3.1.1.7
- UniProt
- P21836
- Ligands
- C56, NAG, CL
- Pockets
- 15 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetylcholinesterase (EC 3.1.1.7) | protein | 535 | 38% helix, 18% strand | P21836 |
| B | Acetylcholinesterase (EC 3.1.1.7) | protein | 533 | 38% helix, 18% strand | P21836 |
Ligands and binding sites
- C56 · 4-(dimethylamino)-N-{[(2R)-1-ethylpyrrolidin-2-yl]methyl}-2-methoxy-5-nitrobenzamide · ligand · 2 copies · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A, B
- CL · Chloride ion · ion · chains B
- PEG · Di(hydroxyethyl)ether · additive · 9 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 8 copies · chains A, B
- 1PE · Pentaethylene glycol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 252 | 0.78 | 0.90 | 36 | C56 |
| 2 | 274 | 0.77 | 0.89 | 35 | C56 |
| 3 | 194 | 0.65 | 0.84 | 24 | 1PE, PEG |
| 4 | 314 | 0.58 | 0.77 | 33 | empty |
| 5 | 169 | 0.58 | 0.82 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 963 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 3 glycan (disulfide, N-glycosylation).
Compared structures
- 4ARA · Mus musculus Acetylcholinesterase in complex with (R)-C5685 at 2.5 A resolution. · the same entry in another collection · chain A against A, TM-score 1.00
- P21836 · AlphaFold monomer V2.0 prediction for acetylcholinesterase (P21836) · a predicted model of the same protein · chain B against A, TM-score 1.00
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 P21836
- Elsewhere: RCSB PDB 4ARA · PDBe 4ARA · UniProt P21836
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.