MolNFT v1 · #24498 · protein
X-ray structure of acetylcholine binding protein (achbp)
1UX2: “X-ray structure of acetylcholine binding protein (achbp)”. X-ray diffraction, 3 ligands (NAG, NH4, SO4), 20 pockets (best druggability 0.78). MolNFT v1 #24498 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1UX2
- Type
- protein
- Length
- 2,065 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylcholine binding protein
- UniProt
- P58154
- Ligands
- NAG, NH4, SO4
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 8% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D, F, H | Acetylcholine binding protein | protein | 207 | 8% helix, 47% strand | P58154 |
| B, E, G, I, J | Acetylcholine binding protein | protein | 206 | 8% helix, 48% strand | P58154 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 10 copies · chains A, H, B, C, F, D, J, E, G, I
- NH4 · Ammonium ion · ion · 4 copies · chains B, C, G, H
- SO4 · Sulfate ion · ion · 2 copies · chains B, C, G, H
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 8 copies · chains A, B, C, D, E, F, G, H, I, J
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 | 818 | 0.78 | 0.81 | 82 | EPE |
| 2 | 480 | 0.76 | 0.84 | 50 | empty |
| 3 | 373 | 0.74 | 0.85 | 46 | EPE |
| 4 | 365 | 0.74 | 0.85 | 44 | EPE |
| 5 | 362 | 0.74 | 0.85 | 44 | SO4, NH4 |
Interfaces
25 interfaces between chains.
- H–I · 1483 Ų buried · 18 hydrogen bonds · protein-protein
- I–J · 1467 Ų buried · 19 hydrogen bonds · protein-protein
- B–C · 1464 Ų buried · 17 hydrogen bonds · protein-protein
- G–H · 1446 Ų buried · 19 hydrogen bonds · protein-protein
- F–J · 1444 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 disulfide, 10 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 P58154
- Elsewhere: RCSB PDB 1UX2 · PDBe 1UX2 · UniProt P58154
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