Research workbench
Fasciculin 2-mouse acetylcholinesterase complex
Analyse Fasciculin 2-mouse acetylcholinesterase complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KU6
- Type
- protein
- Length
- 596 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylcholinesterase; Fasciculin 2
- UniProt
- P21836, P01403
- Ligands
- NAG
- Pockets
- 5 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetylcholinesterase | protein | 535 | 36% helix, 17% strand | P21836 |
| B | Fasciculin 2 | protein | 61 | 0% helix, 44% strand | P01403 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
- EDO · 1,2-ethanediol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 171 | 0.82 | 0.97 | 37 | EDO |
| 2 | 315 | 0.60 | 0.78 | 34 | empty |
| 3 | 161 | 0.48 | 0.77 | 28 | empty |
| 4 | 90 | 0.42 | 0.79 | 14 | empty |
| 5 | 89 | 0.31 | 0.73 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1098 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 disulfide, 1 glycan (disulfide, N-glycosylation).
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
- Every structure of UniProt P01403
- Elsewhere: RCSB PDB 1KU6 · PDBe 1KU6 · UniProt P21836 · UniProt P01403
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