Research workbench
Gsuk channel
Analyse Gsuk channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GX5
- Type
- protein
- Length
- 1,845 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trka domain protein
- UniProt
- Q74FS9
- Ligands
- K, ZN, CA
- Pockets
- 20 · best druggability 0.74
Structure
x-ray diffraction · 4 distinct chains · 47% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trka domain protein | protein | 375 | 53% helix, 13% strand | Q74FS9 |
| B | Trka domain protein | protein | 548 | 44% helix, 18% strand | Q74FS9 |
| C | Trka domain protein | protein | 546 | 43% helix, 18% strand | Q74FS9 |
| D | Trka domain protein | protein | 376 | 52% helix, 13% strand | Q74FS9 |
Ligands and binding sites
- K · Potassium ion · metal · 12 copies · chains A, B, C, D
- ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
- CA · Calcium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1059 | 0.74 | 0.77 | 67 | empty |
| 2 | 1056 | 0.74 | 0.77 | 64 | empty |
| 3 | 616 | 0.69 | 0.78 | 77 | empty |
| 4 | 601 | 0.69 | 0.78 | 76 | empty |
| 5 | 55 | 0.59 | 0.91 | 16 | empty |
Interfaces
2 interfaces between chains.
- A–B · 1780 Ų buried · 12 hydrogen bonds · protein-protein
- C–D · 1759 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 4GX5 · GsuK Channel · 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 Q74FS9
- Elsewhere: RCSB PDB 4GX5 · PDBe 4GX5 · UniProt Q74FS9
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