Research workbench
Single particle cryo-EM structure of the voltage-gated K+ channel EAG1 bound to the channel inhibitor calmodulin
Analyse Single particle cryo-EM structure of the voltage-gated K+ channel EAG1 bound to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5K7L
- Type
- protein
- Length
- 843 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q63472, P62158
- Ligands
- Y01, NAG
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 701 | — | Q63472 |
| B | — | protein | 142 | — | P62158 |
Ligands and binding sites
- Y01 · Cholesterol hemisuccinate · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5K7L · Single particle cryo-EM structure of the voltage-gated K+ channel Eag1 bound to the… · the same entry in another collection · chain A against A, TM-score 1.00
- Q63472 · AlphaFold monomer V2.0 prediction for potassium voltage-gated channel subfamily H member… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q63472
- Every structure of UniProt P62158
- Elsewhere: RCSB PDB 5K7L · PDBe 5K7L · UniProt Q63472 · UniProt P62158
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