Research workbench
Sulfates bound in the vestibule of achbp
Analyse Sulfates bound in the vestibule of achbp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3GUA
- Type
- protein
- Length
- 2,168 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Soluble acetylcholine receptor
- UniProt
- Q8WSF8
- Ligands
- SO4
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D, E, F, H, I, J | Soluble acetylcholine receptor | protein | 217 | 13% helix, 52% strand | Q8WSF8 |
| B, G | Soluble acetylcholine receptor | protein | 216 | 13% helix, 52% strand | Q8WSF8 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 21 copies · chains A, B, E, C, D, F, G, J, H, I
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 | 645 | 0.77 | 0.82 | 57 | SO4 |
| 2 | 677 | 0.76 | 0.82 | 67 | empty |
| 3 | 681 | 0.76 | 0.82 | 59 | SO4 |
| 4 | 698 | 0.76 | 0.81 | 60 | SO4 |
| 5 | 675 | 0.76 | 0.81 | 53 | SO4 |
Interfaces
20 interfaces between chains.
- F–J · 1491 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 1487 Ų buried · 21 hydrogen bonds · protein-protein
- C–D · 1485 Ų buried · 19 hydrogen bonds · protein-protein
- I–J · 1480 Ų buried · 22 hydrogen bonds · protein-protein
- A–E · 1476 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 disulfide (disulfide).
Compared structures
- 3GUA · Sulfates bound in the vestibule of AChBP · the same entry in another collection · 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 Q8WSF8
- Elsewhere: RCSB PDB 3GUA · PDBe 3GUA · UniProt Q8WSF8
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