MolNFT v1 · #25580 · protein
Structure of the tetramerization domain of acetylcholinesterase: four- fold interaction of a www motif with a left-handed polyproline helix
1VZJ: “Structure of the tetramerization domain of acetylcholinesterase: four- fold interaction of a www motif with a…”. X-ray diffraction. MolNFT v1 #25580 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1VZJ
- Type
- protein
- Length
- 278 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P22303, Q9Y215
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 26 | — | P22303 |
| B | — | protein | 31 | — | P22303 |
| C, D, H | — | protein | 32 | — | P22303 |
| E | — | protein | 27 | — | P22303 |
| F, G | — | protein | 34 | — | P22303 |
| I, J | — | protein | 15 | — | Q9Y215 |
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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