MolNFT v1 · #38804 · protein
Crystal structure of mouse acetylcholinesterase complexed with M-(N,N, N-TRIMETHYLAMMONIO)TRIFLUOROACETOPHENONE
2H9Y: “Crystal structure of mouse acetylcholinesterase complexed with M-(N,N…”. X-ray diffraction, 3 ligands (NAF, NAG, FUC), 13 pockets (best druggability 0.76). MolNFT v1 #38804 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 2H9Y
- Type
- protein
- Length
- 1,070 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
- NAF, NAG, FUC
- Pockets
- 13 · best druggability 0.76
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 | 536 | 38% helix, 18% strand | P21836 |
| B | Acetylcholinesterase (EC 3.1.1.7) | protein | 534 | 38% helix, 18% strand | P21836 |
Ligands and binding sites
- NAF · M-(N,N,N-trimethylammonio)-2,2,2-trifluoro-1,1-dihydroxyethylbenzene · ligand · 2 copies · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A, B
- FUC · alpha-L-fucopyranose · sugar · chains A
- P6G · Hexaethylene glycol · additive · chains A, B
- PG4 · Tetraethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 256 | 0.76 | 0.89 | 37 | NAF, PG4 |
| 2 | 239 | 0.74 | 0.88 | 37 | NAF |
| 3 | 394 | 0.63 | 0.78 | 41 | empty |
| 4 | 253 | 0.63 | 0.81 | 33 | P6G |
| 5 | 373 | 0.60 | 0.76 | 37 | empty |
Interfaces
1 interface between chains.
- A–B · 1018 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 3 glycan, 1 covalent (disulfide, N-glycosylation, covalent ligand).
Compared structures
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 2H9Y · PDBe 2H9Y · UniProt P21836
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