Research workbench
Crystal structure of the Y337A mutant of mouse acetylcholinesterase
Analyse Crystal structure of the Y337A mutant of mouse acetylcholinesterase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XUD
- Type
- protein
- Length
- 1,068 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.65
- Source
- MUS MUSCULUS
- Molecule
- Acetylcholinesterase
- EC
- 3.1.1.7
- UniProt
- P21836
- Ligands
- DME
- Pockets
- 13 · best druggability 0.80
Structure
x-ray diffraction · resolution 2.65 · 2 distinct chains · 38% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetylcholinesterase (EC 3.1.1.7) | protein | 537 | 38% helix, 18% strand | P21836 |
| B | Acetylcholinesterase (EC 3.1.1.7) | protein | 531 | 38% helix, 18% strand | P21836 |
Ligands and binding sites
- DME · Decamethonium ion · ligand · chains A
- ACT · Acetate ion · additive · 2 copies · chains A, B
- P6G · Hexaethylene glycol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 386 | 0.80 | 0.88 | 42 | ACT, DME |
| 2 | 332 | 0.79 | 0.89 | 38 | ACT |
| 3 | 343 | 0.68 | 0.82 | 47 | P6G |
| 4 | 201 | 0.58 | 0.81 | 22 | empty |
| 5 | 166 | 0.57 | 0.81 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 928 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 2 covalent (disulfide, additive adduct).
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 2XUD · PDBe 2XUD · UniProt P21836
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