Research workbench
Voltage-dependent K+ channel beta subunit (W121A) in complex with cortisone
Analyse Voltage-dependent K+ channel beta subunit (W121A) in complex with cortisone in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EB3
- Type
- protein
- Length
- 326 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- Rattus norvegicus
- Molecule
- Voltage-gated potassium channel subunit beta-2
- UniProt
- P62483
- Ligands
- NDP, PDN
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · resolution 2 · 1 distinct chain · 52% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Voltage-gated potassium channel subunit beta-2 | protein | 326 | 52% helix, 16% strand | P62483 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- PDN · 17,21-dihydroxypregna-1,4-diene-3,11,20-trione · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 359 | 0.71 | 0.83 | 57 | NDP |
| 2 | 95 | 0.36 | 0.75 | 22 | empty |
Compared structures
- 3EB3 · Voltage-dependent K+ channel beta subunit (W121A) in complex with cortisone · the same entry in another collection · chain A against A, TM-score 1.00
- P62483 · AlphaFold monomer V2.0 prediction for voltage-gated potassium channel subunit beta-2… · a predicted model of the same protein · 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 P62483
- Elsewhere: RCSB PDB 3EB3 · PDBe 3EB3 · UniProt P62483
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