Research workbench
Crystal structure of lymnaea stagnalis acetylcholine binding protein (ls-achbp) complexed with clothianidin
Analyse Crystal structure of lymnaea stagnalis acetylcholine binding protein (ls-achbp)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZJV
- Type
- protein
- Length
- 1,039 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylcholine-binding protein
- UniProt
- P58154
- Ligands
- CT4
- Pockets
- 20 · best druggability 0.76
Structure
x-ray diffraction · 3 distinct chains · 8% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, E | Acetylcholine-binding protein | protein | 208 | 8% helix, 47% strand | P58154 |
| B | Acetylcholine-binding protein | protein | 208 | 8% helix, 47% strand | P58154 |
| C | Acetylcholine-binding protein | protein | 207 | 8% helix, 45% strand | P58154 |
Ligands and binding sites
- CT4 · 1-[(2-chloro-1,3-thiazol-5-yl)methyl]-3-methyl-2-nitroguanidine · ligand · 5 copies · chains A, B, C, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 85 | 0.76 | 0.97 | 20 | CT4 |
| 2 | 111 | 0.75 | 0.94 | 19 | CT4 |
| 3 | 111 | 0.74 | 0.94 | 22 | CT4 |
| 4 | 84 | 0.73 | 0.96 | 20 | CT4 |
| 5 | 182 | 0.69 | 0.87 | 29 | CT4 |
Interfaces
5 interfaces between chains.
- B–C · 1427 Ų buried · 17 hydrogen bonds · protein-protein
- C–D · 1404 Ų buried · 15 hydrogen bonds · protein-protein
- A–E · 1394 Ų buried · 19 hydrogen bonds · protein-protein
- A–B · 1384 Ų buried · 18 hydrogen bonds · protein-protein
- D–E · 1380 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
- 2ZJV · Crystal Structure of Lymnaea stagnalis Acetylcholine Binding Protein (Ls-AChBP) Complexed… · the same entry in another collection · chain E against E, TM-score 1.00
- P58154 · AlphaFold monomer V2.0 prediction for acetylcholine-binding protein (P58154) · a predicted model of the same protein · chain E against A, TM-score 0.98
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 2ZJV · PDBe 2ZJV · UniProt P58154
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