MolNFT v1 · #176973 · protein
Crystal structure of human acetylcholinesterase in complex with donepezil
7E3H: “Crystal structure of human acetylcholinesterase in complex with donepezil”. X-ray diffraction, 3 ligands (E20, NAG, FUC). MolNFT v1 #176973 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7E3H
- Type
- protein
- Length
- 1,054 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P22303
- Ligands
- E20, NAG, FUC
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 527 | — | P22303 |
Ligands and binding sites
- E20 · 1-benzyl-4-[(5,6-dimethoxy-1-indanon-2-yl) methyl]piperidine · ligand · 2 copies · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B
- FUC · alpha-L-fucopyranose · sugar · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7E3H · Crystal structure of human acetylcholinesterase in complex with donepezil · the same entry in another collection · chain A against A, TM-score 1.00
- P22303 · AlphaFold monomer V2.0 prediction for acetylcholinesterase (P22303) · 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 P22303
- Elsewhere: RCSB PDB 7E3H · PDBe 7E3H · UniProt P22303
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