Research workbench
Solution structure of the eag domain of the herg (KV11.1) K+ channel
Analyse Solution structure of the eag domain of the herg (KV11.1) K+ channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2L1M
- Type
- protein
- Length
- 135 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Potassium voltage-gated channel subfamily H member 2
- UniProt
- Q12809
- Pockets
- 1 · best druggability 0.50
Structure
solution nmr · 1 distinct chain · 29% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Potassium voltage-gated channel subfamily H member 2 | protein | 135 | 29% helix, 18% strand | Q12809 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 58 | 0.50 | 0.86 | 15 | empty |
Compared structures
- 2L1M · Solution structure of the eag domain of the hERG (Kv11.1) K+ channel · the same entry in another collection · chain A against A, TM-score 1.00
- Q12809 · 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 0.70
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 Q12809
- Elsewhere: RCSB PDB 2L1M · PDBe 2L1M · UniProt Q12809
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