MolNFT v1 · #8061 · protein
Structure of acetylcholinesterase complex with (+)-huperzine a at 2.1A resolution
1GPK: “Structure of acetylcholinesterase complex with (+)-huperzine a at 2.1A resolution”. X-ray diffraction, 2 ligands (HUP, NAG), 4 pockets (best druggability 0.76). MolNFT v1 #8061 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 1GPK
- Type
- protein
- Length
- 529 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylcholinesterase
- EC
- 3.1.1.7
- UniProt
- P04058
- Ligands
- HUP, NAG
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetylcholinesterase (EC 3.1.1.7) | protein | 529 | 39% helix, 18% strand | P04058 |
Ligands and binding sites
- HUP · Huperzine A · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 315 | 0.76 | 0.87 | 39 | HUP |
| 2 | 314 | 0.56 | 0.76 | 32 | empty |
| 3 | 122 | 0.46 | 0.78 | 15 | empty |
| 4 | 56 | 0.35 | 0.78 | 12 | empty |
Modifications
Observed in the structure: 3 disulfide, 3 glycan (disulfide, N-glycosylation).
Compared structures
- 1GPK · Structure of Acetylcholinesterase Complex with (+)-Huperzine A at 2.1A Resolution · the same entry in another collection · chain A against A, TM-score 1.00
- P04058 · AlphaFold monomer V2.0 prediction for acetylcholinesterase (P04058) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 P04058
- Elsewhere: RCSB PDB 1GPK · PDBe 1GPK · UniProt P04058
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