Research workbench
Complex structure of FAB35 and human nachr ALPHA1
Analyse Complex structure of FAB35 and human nachr ALPHA1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HBT
- Type
- protein
- Length
- 717 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylcholine receptor subunit alpha 1; FAB35, light chain; FAB35, heavy chain…
- UniProt
- G5E9G9, P60616
- Ligands
- MAN, NAG, BMA
- Pockets
- 6 · best druggability 0.64
Structure
x-ray diffraction · 4 distinct chains · 8% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Acetylcholine receptor subunit alpha 1 | protein | 212 | 10% helix, 48% strand | G5E9G9 |
| C | FAB35, light chain | protein | 212 | 4% helix, 52% strand | — |
| D | FAB35, heavy chain | protein | 219 | 10% helix, 52% strand | — |
| A | Alpha-bungarotoxin isoform V31 | protein | 74 | 5% helix, 31% strand | P60616 |
Ligands and binding sites
- MAN · alpha-D-mannopyranose · sugar · 6 copies · chains B, A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains B
- BMA · beta-D-mannopyranose · sugar · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 617 | 0.64 | 0.75 | 52 | empty |
| 2 | 345 | 0.58 | 0.76 | 41 | empty |
| 3 | 107 | 0.37 | 0.74 | 21 | empty |
| 4 | 63 | 0.33 | 0.76 | 12 | empty |
| 5 | 58 | 0.29 | 0.75 | 17 | empty |
Interfaces
4 interfaces between chains.
- C–D · 1791 Ų buried · 14 hydrogen bonds · protein-protein
- B–A · 800 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 669 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 340 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 disulfide, 1 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 G5E9G9
- Every structure of UniProt P60616
- Elsewhere: RCSB PDB 5HBT · PDBe 5HBT · UniProt G5E9G9 · UniProt P60616
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