Research workbench
Rigidity of loop 1 contributes to equipotency of globular and ribbon isomers of alpha-conotoxin ausia
Analyse Rigidity of loop 1 contributes to equipotency of globular and ribbon isomers of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7N0Y
- Type
- protein
- Length
- 1,030 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylcholine-binding protein; Globular alpha-conotoxin ausia
- UniProt
- P58154, P0DL39
- Pockets
- 19 · best druggability 0.73
Structure
x-ray diffraction · 5 distinct chains · 8% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Acetylcholine-binding protein | protein | 205 | 7% helix, 47% strand | P58154 |
| C | Acetylcholine-binding protein | protein | 204 | 8% helix, 47% strand | P58154 |
| D | Acetylcholine-binding protein | protein | 200 | 9% helix, 46% strand | P58154 |
| E | Acetylcholine-binding protein | protein | 202 | 7% helix, 48% strand | P58154 |
| G | Globular alpha-conotoxin ausia | protein | 14 | 43% helix, 0% strand | P0DL39 |
Pockets
19 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 141 | 0.73 | 0.91 | 25 | empty |
| 2 | 140 | 0.71 | 0.90 | 23 | empty |
| 3 | 150 | 0.70 | 0.89 | 25 | empty |
| 4 | 420 | 0.69 | 0.80 | 52 | empty |
| 5 | 431 | 0.68 | 0.80 | 43 | empty |
Interfaces
7 interfaces between chains.
- C–D · 1491 Ų buried · 19 hydrogen bonds · protein-protein
- A–C · 1376 Ų buried · 16 hydrogen bonds · protein-protein
- B–D · 1369 Ų buried · 16 hydrogen bonds · protein-protein
- A–E · 1308 Ų buried · 17 hydrogen bonds · protein-protein
- B–E · 1133 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
- 7N0Y · Rigidity of loop 1 contributes to equipotency of globular and ribbon isomers of… · the same entry in another collection · chain G against G, 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 0.98
- P0DL39 · AlphaFold monomer V2.0 prediction for alpha-conotoxin ausia (P0DL39) · a predicted model of the same protein · chain G against A, TM-score 0.34
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
- Every structure of UniProt P0DL39
- Elsewhere: RCSB PDB 7N0Y · PDBe 7N0Y · UniProt P58154 · UniProt P0DL39
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