Research workbench
Single particle cryo-EM structure of the voltage-gated K+ channel EAG1 3-13 deletion mutant bound to calmodulin (conformation 2)
Analyse Single particle cryo-EM structure of the voltage-gated K+ channel EAG1 3-13… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PBX
- Type
- protein
- Length
- 3,152 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q63472, P0DP23
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G | — | protein | 648 | — | Q63472 |
| B, D, F, H | — | protein | 140 | — | P0DP23 |
Compared structures
- 6PBX · Single particle cryo-EM structure of the voltage-gated K+ channel Eag1 3-13 deletion… · the same entry in another collection · chain H against H, 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
- P0DP23 · AlphaFold monomer V2.0 prediction for calmodulin-1 (P0DP23) · a predicted model of the same protein · chain D against A, TM-score 0.48
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 P0DP23
- Elsewhere: RCSB PDB 6PBX · PDBe 6PBX · UniProt Q63472 · UniProt P0DP23
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