MolNFT v1 · #6314 · protein
Crystal structure of mutant E202Q of human acetylcholinesterase complexed with green mamba venom peptide fasciculin-II
1F8U: “Crystal structure of mutant E202Q of human acetylcholinesterase complexed with green mamba venom peptide…”. X-ray diffraction, 1 ligand (NAG), 8 pockets (best druggability 0.82). MolNFT v1 #6314 on GenesisL1: 3D structure, binding…
- PDB
- 1F8U
- Type
- protein
- Length
- 592 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylcholinesterase; Fasciculin II
- EC
- 3.1.1.7
- UniProt
- P22303, P01403
- Ligands
- NAG
- Pockets
- 8 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetylcholinesterase (EC 3.1.1.7) | protein | 531 | 38% helix, 18% strand | P22303 |
| B | Fasciculin II | protein | 61 | 0% helix, 44% strand | P01403 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 165 | 0.82 | 0.97 | 35 | empty |
| 2 | 335 | 0.58 | 0.76 | 37 | empty |
| 3 | 94 | 0.50 | 0.82 | 16 | empty |
| 4 | 93 | 0.42 | 0.78 | 19 | empty |
| 5 | 105 | 0.40 | 0.76 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1165 Ų buried · 27 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 1F8U · Crystal structure of mutant E202Q of human acetylcholinesterase complexed with green… · 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 A 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
- Every structure of UniProt P01403
- Elsewhere: RCSB PDB 1F8U · PDBe 1F8U · UniProt P22303 · UniProt P01403
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