MolNFT v1 · #14469 · protein
Mouse acetylcholinesterase catalytic domain, glycosylated protein
1MAA: “Mouse acetylcholinesterase catalytic domain, glycosylated protein”. X-ray diffraction, 4 ligands (DME, NAG, FUL), 20 pockets (best druggability 0.85). MolNFT v1 #14469 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1MAA
- Type
- protein
- Length
- 2,157 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylcholinesterase
- EC
- 3.1.1.7
- UniProt
- P21836
- Ligands
- DME, NAG, FUL, PO4
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 4 distinct chains · 37% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetylcholinesterase (EC 3.1.1.7) | protein | 540 | 37% helix, 16% strand | P21836 |
| B | Acetylcholinesterase (EC 3.1.1.7) | protein | 536 | 38% helix, 17% strand | P21836 |
| C | Acetylcholinesterase (EC 3.1.1.7) | protein | 540 | 38% helix, 17% strand | P21836 |
| D | Acetylcholinesterase (EC 3.1.1.7) | protein | 541 | 37% helix, 17% strand | P21836 |
Ligands and binding sites
- DME · Decamethonium ion · ligand · 4 copies · chains A, B, D, C
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains D, A
- FUL · beta-L-fucopyranose · sugar · chains D
- PO4 · Phosphate ion · ion · 3 copies · chains B, C, A
- GOL · Glycerol · additive · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 321 | 0.85 | 0.95 | 50 | DME |
| 2 | 305 | 0.84 | 0.94 | 50 | DME |
| 3 | 269 | 0.74 | 0.87 | 37 | DME |
| 4 | 266 | 0.72 | 0.86 | 37 | DME |
| 5 | 362 | 0.60 | 0.77 | 34 | empty |
Interfaces
5 interfaces between chains.
- C–D · 1021 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 992 Ų buried · 10 hydrogen bonds · protein-protein
- B–D · 639 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 622 Ų buried · 3 hydrogen bonds · protein-protein
- A–D · 28 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 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 P21836
- Elsewhere: RCSB PDB 1MAA · PDBe 1MAA · UniProt P21836
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.