MolNFT v1 · #83451 · protein
Crystal structure of acetylcholine bound to ls-achbp
3WIP · Acetylcholine-binding protein: “Crystal structure of acetylcholine bound to ls-achbp”. X-ray diffraction, 2 ligands (ACH, SO4), 20 pockets (best druggability 0.84). MolNFT v1 #83451 on GenesisL1: 3D structure, binding sites and…
- PDB
- 3WIP
- Type
- protein
- Length
- 2,023 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylcholine-binding protein
- UniProt
- P58154
- Ligands
- ACH, SO4
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 8 distinct chains · 8% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E | Acetylcholine-binding protein | protein | 202 | 8% helix, 49% strand | P58154 |
| B | Acetylcholine-binding protein | protein | 208 | 8% helix, 47% strand | P58154 |
| C | Acetylcholine-binding protein | protein | 202 | 8% helix, 49% strand | P58154 |
| D, G | Acetylcholine-binding protein | protein | 202 | 8% helix, 49% strand | P58154 |
| F | Acetylcholine-binding protein | protein | 206 | 8% helix, 48% strand | P58154 |
| H | Acetylcholine-binding protein | protein | 198 | 9% helix, 49% strand | P58154 |
| I | Acetylcholine-binding protein | protein | 200 | 8% helix, 50% strand | P58154 |
| J | Acetylcholine-binding protein | protein | 201 | 8% helix, 49% strand | P58154 |
Ligands and binding sites
- ACH · Acetylcholine · ligand · 10 copies · chains A, B, C, D, E, F, G, H, I, J
- SO4 · Sulfate ion · ion · 7 copies · chains A, B, C, D, F, J, E, G
- 1PE · Pentaethylene glycol · additive · 12 copies · chains A, H, E, B, C, G, D, F, I, J
- ACT · Acetate ion · additive · 3 copies · chains A, B, G, H
- GOL · Glycerol · additive · chains B, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1068 | 0.84 | 0.85 | 105 | 1PE, SO4 |
| 2 | 752 | 0.80 | 0.83 | 97 | ACH, 1PE |
| 3 | 871 | 0.79 | 0.81 | 97 | ACH, 1PE |
| 4 | 1097 | 0.78 | 0.80 | 66 | SO4, 1PE |
| 5 | 1012 | 0.78 | 0.80 | 75 | 1PE |
Interfaces
20 interfaces between chains.
- F–J · 1416 Ų buried · 19 hydrogen bonds · protein-protein
- F–G · 1384 Ų buried · 22 hydrogen bonds · protein-protein
- D–E · 1371 Ų buried · 17 hydrogen bonds · protein-protein
- G–H · 1365 Ų buried · 18 hydrogen bonds · protein-protein
- I–J · 1354 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 17 disulfide (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 P58154
- Elsewhere: RCSB PDB 3WIP · PDBe 3WIP · UniProt P58154
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