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Structure of tabun inhibited acetylcholinesterase in complex with 2- ((HYDROXYIMINO)METHYL)-1-(5-(4-methyl-3-NITROBENZAMIDO)PENTYL) pyridinium
Analyse Structure of tabun inhibited acetylcholinesterase in complex with 2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7R2F
- Type
- protein
- Length
- 1,069 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylcholinesterase
- EC
- 3.1.1.7
- UniProt
- P21836
- Ligands
- I1X, 7PG, NAG
- Pockets
- 13 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetylcholinesterase (EC 3.1.1.7) | protein | 536 | 38% helix, 18% strand | P21836 |
| B | Acetylcholinesterase (EC 3.1.1.7) | protein | 533 | 39% helix, 18% strand | P21836 |
Ligands and binding sites
- I1X · 4-methyl-3-nitro-~{N}-[(2~{E},4~{E})-5-[2-[(oxidanylamino)methyl]pyridin-1-yl]penta-2,4-dienyl]benzamide · ligand · 2 copies · chains A, B
- 7PG · 2,5,8,11,14,17,20,23-octaoxapentacosan-25-ol · ligand · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
- PG0 · 2-(2-methoxyethoxy)ethanol · additive · 14 copies · 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 | 205 | 0.79 | 0.93 | 35 | I1X |
| 2 | 235 | 0.79 | 0.92 | 39 | I1X |
| 3 | 258 | 0.64 | 0.82 | 36 | PG0, 7PG |
| 4 | 185 | 0.58 | 0.81 | 22 | PG0 |
| 5 | 186 | 0.57 | 0.81 | 20 | PG0 |
Interfaces
1 interface between chains.
- A–B · 973 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 2 glycan, 2 modified (disulfide, N-glycosylation, nonstandard).
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 7R2F · PDBe 7R2F · UniProt P21836
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