Research workbench
Structure of the eag domain-cnbhd complex of the mouse EAG1 channel
Analyse Structure of the eag domain-cnbhd complex of the mouse EAG1 channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LLO
- Type
- protein
- Length
- 1,143 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Potassium voltage-gated channel subfamily H member 1
- UniProt
- Q60603
- Pockets
- 13 · best druggability 0.80
Structure
x-ray diffraction · 7 distinct chains · 27% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Potassium voltage-gated channel subfamily H member 1 | protein | 173 | 31% helix, 29% strand | Q60603 |
| B, F | Potassium voltage-gated channel subfamily H member 1 | protein | 121 | 26% helix, 36% strand | Q60603 |
| C | Potassium voltage-gated channel subfamily H member 1 | protein | 168 | 26% helix, 29% strand | Q60603 |
| D | Potassium voltage-gated channel subfamily H member 1 | protein | 110 | 24% helix, 39% strand | Q60603 |
| E | Potassium voltage-gated channel subfamily H member 1 | protein | 171 | 29% helix, 29% strand | Q60603 |
| G | Potassium voltage-gated channel subfamily H member 1 | protein | 169 | 27% helix, 29% strand | Q60603 |
| H | Potassium voltage-gated channel subfamily H member 1 | protein | 110 | 25% helix, 39% strand | Q60603 |
Pockets
13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 754 | 0.80 | 0.84 | 79 | empty |
| 2 | 667 | 0.78 | 0.83 | 81 | empty |
| 3 | 373 | 0.78 | 0.88 | 49 | empty |
| 4 | 748 | 0.74 | 0.79 | 62 | empty |
| 5 | 275 | 0.66 | 0.82 | 32 | empty |
Interfaces
16 interfaces between chains.
- E–F · 808 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 734 Ų buried · 7 hydrogen bonds · protein-protein
- G–H · 665 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 656 Ų buried · 8 hydrogen bonds · protein-protein
- A–F · 418 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 4LLO · Structure of the eag domain-CNBHD complex of the mouse EAG1 channel · the same entry in another collection · chain H against H, TM-score 1.00
- Q60603 · AlphaFold monomer V2.0 prediction for potassium voltage-gated channel subfamily H member… · a predicted model of the same protein · chain H against A, TM-score 0.99
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 Q60603
- Elsewhere: RCSB PDB 4LLO · PDBe 4LLO · UniProt Q60603
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