Research workbench
X-ray crystal structure of lymnaea stagnalis acetylcholine binding protein (lsachbp) in complex with 2-thiophenylmethylene anabaseine (2TAB)
Analyse X-ray crystal structure of lymnaea stagnalis acetylcholine binding protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ZJT
- Type
- protein
- Length
- 2,115 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylcholine-binding protein
- UniProt
- P58154
- Ligands
- 4P6, PO4
- Pockets
- 20 · best druggability 0.72
Structure
x-ray diffraction · 8 distinct chains · 10% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E | Acetylcholine-binding protein | protein | 212 | 9% helix, 46% strand | P58154 |
| B | Acetylcholine-binding protein | protein | 210 | 10% helix, 46% strand | P58154 |
| C | Acetylcholine-binding protein | protein | 209 | 11% helix, 45% strand | P58154 |
| D | Acetylcholine-binding protein | protein | 214 | 11% helix, 45% strand | P58154 |
| F | Acetylcholine-binding protein | protein | 214 | 9% helix, 46% strand | P58154 |
| G | Acetylcholine-binding protein | protein | 214 | 9% helix, 44% strand | P58154 |
| H | Acetylcholine-binding protein | protein | 208 | 10% helix, 47% strand | P58154 |
| I, J | Acetylcholine-binding protein | protein | 211 | 9% helix, 48% strand | P58154 |
Ligands and binding sites
- 4P6 · (3E)-3-(thiophen-2-ylmethylidene)-3,4,5,6-tetrahydro-2,3'-bipyridine · ligand · 10 copies · chains A, B, C, D, E, F, G, H, I, J
- PO4 · Phosphate ion · ion · 10 copies · chains A, E, B, C, D, 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 | 210 | 0.72 | 0.88 | 27 | 4P6 |
| 2 | 185 | 0.72 | 0.89 | 32 | 4P6 |
| 3 | 227 | 0.70 | 0.86 | 25 | 4P6 |
| 4 | 347 | 0.69 | 0.82 | 31 | 4P6 |
| 5 | 210 | 0.69 | 0.86 | 25 | 4P6 |
Interfaces
20 interfaces between chains.
- H–I · 1635 Ų buried · 27 hydrogen bonds · protein-protein
- F–G · 1634 Ų buried · 25 hydrogen bonds · protein-protein
- B–C · 1628 Ų buried · 27 hydrogen bonds · protein-protein
- F–J · 1587 Ų buried · 26 hydrogen bonds · protein-protein
- I–J · 1587 Ų buried · 22 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 disulfide (disulfide).
Compared structures
- 4ZJT · X-ray crystal structure of Lymnaea stagnalis acetylcholine binding protein (LsAChBP) in… · the same entry in another collection · chain J against J, TM-score 1.00
- P58154 · AlphaFold monomer V2.0 prediction for acetylcholine-binding protein (P58154) · a predicted model of the same protein · chain B against A, TM-score 0.94
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 4ZJT · PDBe 4ZJT · UniProt P58154
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.