Research workbench
Structure of the tetramerization domain of acetylcholinesterase: four- fold interaction of a www motif with a left-handed polyproline helix
Analyse Structure of the tetramerization domain of acetylcholinesterase: four- fold… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VZJ
- Type
- protein
- Length
- 278 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylcholinesterase; Acetylcholinesterase collagenic tail peptide
- EC
- 3.1.1.7
- UniProt
- P22303, Q9Y215
- Pockets
- 4 · best druggability 0.56
Structure
x-ray diffraction · 6 distinct chains · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetylcholinesterase (EC 3.1.1.7) | protein | 26 | 85% helix, 0% strand | P22303 |
| B | Acetylcholinesterase (EC 3.1.1.7) | protein | 31 | 90% helix, 0% strand | P22303 |
| C, D, H | Acetylcholinesterase (EC 3.1.1.7) | protein | 32 | 94% helix, 0% strand | P22303 |
| E | Acetylcholinesterase (EC 3.1.1.7) | protein | 27 | 74% helix, 0% strand | P22303 |
| F, G | Acetylcholinesterase (EC 3.1.1.7) | protein | 34 | 91% helix, 0% strand | P22303 |
| I, J | Acetylcholinesterase collagenic tail peptide | protein | 15 | 0% helix, 0% strand | Q9Y215 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 71 | 0.56 | 0.87 | 12 | empty |
| 2 | 158 | 0.49 | 0.77 | 20 | empty |
| 3 | 98 | 0.42 | 0.78 | 16 | empty |
| 4 | 63 | 0.31 | 0.75 | 15 | empty |
Interfaces
18 interfaces between chains.
- D–I · 638 Ų buried · 7 hydrogen bonds · protein-protein
- H–J · 623 Ų buried · 6 hydrogen bonds · protein-protein
- G–J · 616 Ų buried · 5 hydrogen bonds · protein-protein
- G–H · 595 Ų buried · 1 hydrogen bond · protein-protein
- C–D · 592 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 1VZJ · Structure of the tetramerization domain of acetylcholinesterase: four-fold interaction of… · the same entry in another collection · chain J against J, TM-score 1.00
- P22303 · AlphaFold monomer V2.0 prediction for acetylcholinesterase (P22303) · a predicted model of the same protein · chain G against A, TM-score 0.87
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 Q9Y215
- Elsewhere: RCSB PDB 1VZJ · PDBe 1VZJ · UniProt P22303 · UniProt Q9Y215
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