MolNFT v1 · #147961 · protein
Human butyrylcholinesterase in complex with thioflavine T
6ESY: “Human butyrylcholinesterase in complex with thioflavine T”. X-ray diffraction, 4 ligands (TFX, NAG, FUC), 14 pockets (best druggability 0.78). MolNFT v1 #147961 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6ESY
- Type
- protein
- Length
- 1,053 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cholinesterase
- EC
- 3.1.1.8
- UniProt
- P06276
- Ligands
- TFX, NAG, FUC, CL
- Pockets
- 14 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cholinesterase (EC 3.1.1.8) | protein | 527 | 34% helix, 17% strand | P06276 |
| B | Cholinesterase (EC 3.1.1.8) | protein | 526 | 35% helix, 16% strand | P06276 |
Ligands and binding sites
- TFX · 2-[4-(dimethylamino)phenyl]-3,6-dimethyl-1,3-benzothiazol-3-ium · ligand · 4 copies · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 18 copies · chains A, B
- FUC · alpha-L-fucopyranose · sugar · 3 copies · chains A, B
- CL · Chloride ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 565 | 0.78 | 0.84 | 46 | TFX |
| 2 | 553 | 0.78 | 0.84 | 46 | TFX |
| 3 | 328 | 0.57 | 0.76 | 40 | empty |
| 4 | 220 | 0.55 | 0.78 | 26 | empty |
| 5 | 176 | 0.51 | 0.78 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 720 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 13 glycan, 6 disulfide (N-glycosylation, disulfide).
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 P06276
- Elsewhere: RCSB PDB 6ESY · PDBe 6ESY · UniProt P06276
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