MolNFT v1 · #8102 · protein
Acetylcholinesterase (E.C. 3.1.1.7) complexed with nap
1GQS: “Acetylcholinesterase (E.C. 3.1.1.7) complexed with nap”. X-ray diffraction, 2 ligands (SAF, NAG), 5 pockets (best druggability 0.76). MolNFT v1 #8102 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1GQS
- Type
- protein
- Length
- 532 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
- SAF, NAG
- Pockets
- 5 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetylcholinesterase (EC 3.1.1.7) | protein | 532 | 38% helix, 17% strand | P04058 |
Ligands and binding sites
- SAF · 3-[(1S)-1-(dimethylamino)ethyl]phenol · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
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 | 317 | 0.76 | 0.87 | 39 | SAF |
| 2 | 321 | 0.56 | 0.75 | 32 | empty |
| 3 | 77 | 0.40 | 0.78 | 15 | empty |
| 4 | 54 | 0.31 | 0.77 | 13 | empty |
| 5 | 64 | 0.30 | 0.74 | 18 | empty |
Modifications
Observed in the structure: 3 disulfide, 2 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 P04058
- Elsewhere: RCSB PDB 1GQS · PDBe 1GQS · UniProt P04058
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