MolNFT v1 · #86616 · protein
Structure of mouse acetylcholinesterase inhibited by cbdp (12-H soak) : cresyl-phosphoserine adduct
4BC0: “Structure of mouse acetylcholinesterase inhibited by cbdp (12-H soak) : cresyl-phosphoserine adduct”. X-ray diffraction, 4 ligands (4OJ, NAG, SO4), 20 pockets (best druggability 0.85). MolNFT v1 #86616 on GenesisL1: 3D structure…
- PDB
- 4BC0
- Type
- protein
- Length
- 2,161 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
- 4OJ, NAG, SO4, CL
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 3 distinct chains · 36% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetylcholinesterase (EC 3.1.1.7) | protein | 542 | 36% helix, 15% strand | P21836 |
| B | Acetylcholinesterase (EC 3.1.1.7) | protein | 539 | 37% helix, 17% strand | P21836 |
| C, D | Acetylcholinesterase (EC 3.1.1.7) | protein | 540 | 37% helix, 17% strand | P21836 |
Ligands and binding sites
- 4OJ · (2-methylphenyl) dihydrogen phosphate · ligand · 4 copies · chains A, B, C, D
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 7 copies · chains A, B, C, D
- SO4 · Sulfate ion · ion · 13 copies · chains A, B, C, D
- CL · Chloride ion · ion · 8 copies · chains 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, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 349 | 0.85 | 0.94 | 55 | 4OJ |
| 2 | 357 | 0.84 | 0.93 | 58 | 4OJ |
| 3 | 272 | 0.74 | 0.87 | 34 | 4OJ |
| 4 | 271 | 0.72 | 0.86 | 40 | 4OJ |
| 5 | 485 | 0.65 | 0.77 | 53 | SO4 |
Interfaces
4 interfaces between chains.
- A–B · 1036 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 1004 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 580 Ų buried · 7 hydrogen bonds · protein-protein
- A–D · 573 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 disulfide, 7 glycan, 4 covalent (disulfide, N-glycosylation, covalent ligand).
Compared structures
- 4BC0 · Structure of mouse acetylcholinesterase inhibited by CBDP (12-h soak)… · the same entry in another collection · chain D against D, TM-score 1.00
- P21836 · AlphaFold monomer V2.0 prediction for acetylcholinesterase (P21836) · a predicted model of the same protein · chain D 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 P21836
- Elsewhere: RCSB PDB 4BC0 · PDBe 4BC0 · UniProt P21836
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