MolNFT v1 · #119229 · protein
Structure of homo sapiens acetylcholinesterase phosphonylated by sarin.
5FPQ: “Structure of homo sapiens acetylcholinesterase phosphonylated by sarin.”. X-ray diffraction, 14 pockets (best druggability 0.74). MolNFT v1 #119229 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5FPQ
- Type
- protein
- Length
- 1,062 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylcholinesterase
- EC
- 3.1.1.7
- UniProt
- P22303
- Pockets
- 14 · best druggability 0.74
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 | 532 | 38% helix, 17% strand | P22303 |
| B | Acetylcholinesterase (EC 3.1.1.7) | protein | 530 | 38% helix, 18% strand | P22303 |
Ligands and binding sites
- 1PE · Pentaethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 79 | 0.74 | 0.97 | 23 | empty |
| 2 | 760 | 0.70 | 0.77 | 84 | empty |
| 3 | 192 | 0.68 | 0.86 | 35 | empty |
| 4 | 299 | 0.59 | 0.78 | 33 | empty |
| 5 | 264 | 0.55 | 0.77 | 32 | empty |
Interfaces
1 interface between chains.
- A–B · 413 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 2 modified (disulfide, nonstandard).
Compared structures
- 5FPQ · Structure of Homo sapiens acetylcholinesterase phosphonylated by sarin. · the same entry in another collection · chain A against A, TM-score 1.00
- P22303 · AlphaFold monomer V2.0 prediction for acetylcholinesterase (P22303) · a predicted model of the same protein · chain B 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 P22303
- Elsewhere: RCSB PDB 5FPQ · PDBe 5FPQ · UniProt P22303
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