MolNFT v1 · #51496 · protein
Structure of the complex of tcache with 1-(2-nitrophenyl)-2,2,2- trifluoroethyl-arsenocholine after a 9 seconds annealing to room temperature, during the first 5 seconds of which laser irradiation at 266NM took place
2V98 · Acetylcholinesterase: “Structure of the complex of tcache with 1-(2-nitrophenyl)-2,2,2- trifluoroethyl-arsenocholine after a 9…”. X-ray diffraction, 3 ligands (CFQ, NAG, CL), 11 pockets (best druggability 0.77). MolNFT v1 #51496 on…
- PDB
- 2V98
- Type
- protein
- Length
- 1,060 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylcholinesterase
- EC
- 3.1.1.7
- UniProt
- P04058
- Ligands
- CFQ, NAG, CL
- Pockets
- 11 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetylcholinesterase (EC 3.1.1.7) | protein | 528 | 38% helix, 16% strand | P04058 |
| B | Acetylcholinesterase (EC 3.1.1.7) | protein | 532 | 37% helix, 16% strand | P04058 |
Ligands and binding sites
- CFQ · 1-(2-nitrophenyl)-2,2,2-trifluoroethyl]-arsenocholine · ligand · 4 copies · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 330 | 0.77 | 0.88 | 35 | CFQ |
| 2 | 376 | 0.76 | 0.85 | 36 | CFQ |
| 3 | 333 | 0.58 | 0.76 | 35 | empty |
| 4 | 328 | 0.57 | 0.76 | 33 | empty |
| 5 | 127 | 0.47 | 0.78 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 924 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 4 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 2V98 · PDBe 2V98 · UniProt P04058
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