Research workbench
Cryo-EM structure of AdTx1-alpha1AAR-Nb6
Analyse Cryo-EM structure of AdTx1-alpha1AAR-Nb6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 8HN1
- Type
- protein
- Length
- 456 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.9
- Source
- Dendroaspis angusticeps; Homo sapiens; Lama glama
- Molecule
- Toxin AdTx1; Alpha-1A adrenergic receptor; Nb6
- UniProt
- P85092, P35348
- Pockets
- 4 · best druggability 0.85
Structure
electron microscopy · resolution 2.9 · 3 distinct chains · 49% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | Toxin AdTx1 | protein | 65 | 0% helix, 43% strand | P85092 |
| A | Alpha-1A adrenergic receptor | protein | 280 | 80% helix, 0% strand | P35348 |
| D | Nb6 | protein | 111 | 0% helix, 41% strand | — |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 425 | 0.85 | 0.92 | 53 | empty |
| 2 | 61 | 0.66 | 0.94 | 17 | empty |
| 3 | 223 | 0.60 | 0.81 | 29 | empty |
| 4 | 59 | 0.34 | 0.78 | 16 | empty |
Interfaces
2 interfaces between chains.
- C–A · 1211 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 620 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- P35348 · AlphaFold monomer V2.0 prediction for alpha-1A adrenergic receptor (P35348) · a predicted model of the same protein · chain A against A, TM-score 0.94
- P85092 · AlphaFold monomer V2.0 prediction for toxin ADTX1 (P85092) · a predicted model of the same protein · chain C against A, TM-score 0.92
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 P85092
- Every structure of UniProt P35348
- Elsewhere: RCSB PDB 8HN1 · PDBe 8HN1 · UniProt P85092 · UniProt P35348
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