Research workbench
Structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis
Analyse Structures of ligand bound human choline acetyltransferase provide insight into… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FY5
- Type
- protein
- Length
- 577 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Choline O-acetyltransferase
- EC
- 2.3.1.6
- UniProt
- P28329
- Ligands
- SOP
- Pockets
- 9 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Choline O-acetyltransferase (EC 2.3.1.6) | protein | 577 | 47% helix, 14% strand | P28329 |
Ligands and binding sites
- SOP · [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]methyl (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-{[3-oxo-3-({2-[(2-oxopropyl)thio]ethyl}amino)propyl]amino}butyl dihydrogen diphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 805 | 0.81 | 0.83 | 82 | SOP |
| 2 | 114 | 0.49 | 0.80 | 19 | empty |
| 3 | 72 | 0.44 | 0.81 | 19 | empty |
| 4 | 98 | 0.43 | 0.78 | 22 | empty |
| 5 | 86 | 0.41 | 0.78 | 21 | empty |
Compared structures
- 2FY5 · Structures of ligand bound human choline acetyltransferase provide insight into… · the same entry in another collection · chain A against A, TM-score 1.00
- P28329 · AlphaFold monomer V2.0 prediction for choline O-acetyltransferase (P28329) · a predicted model of the same protein · chain A 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 P28329
- Elsewhere: RCSB PDB 2FY5 · PDBe 2FY5 · UniProt P28329
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