Research workbench
X-ray structure of human butyrylcholinesterase inhibited by racemic vx
Analyse X-ray structure of human butyrylcholinesterase inhibited by racemic vx in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XQF
- Type
- protein
- Length
- 527 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cholinesterase
- EC
- 3.1.1.8
- UniProt
- P06276
- Ligands
- GLY, VX, NAG, FUL, NA, K, UNX, CL, SO4
- Pockets
- 5 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cholinesterase (EC 3.1.1.8) | protein | 527 | 38% helix, 17% strand | P06276 |
Ligands and binding sites
- GLY · Glycine · ligand · chains A
- VX · O-ethylmethylphosphonic acid ester group · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A
- FUL · beta-L-fucopyranose · sugar · 2 copies · chains A
- NA · Sodium ion · metal · chains A
- K · Potassium ion · metal · chains A
- UNX · Unknown atom or ion · ion · 36 copies · chains A
- CL · Chloride ion · ion · 2 copies · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 559 | 0.78 | 0.85 | 46 | UNX, VX |
| 2 | 585 | 0.68 | 0.77 | 44 | UNX |
| 3 | 69 | 0.42 | 0.80 | 15 | empty |
| 4 | 133 | 0.42 | 0.75 | 28 | UNX |
| 5 | 69 | 0.36 | 0.77 | 19 | UNX |
Modifications
Observed in the structure: 6 glycan, 3 disulfide, 1 covalent (N-glycosylation, disulfide, covalent ligand).
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 2XQF · PDBe 2XQF · UniProt P06276
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