Research workbench
Crystal structure of pas domain from the human erg (herg) potassium channel
Analyse Crystal structure of pas domain from the human erg (herg) potassium channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HQA
- Type
- protein
- Length
- 110 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Potassium voltage-gated channel subfamily H member 2
- UniProt
- Q12809
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Potassium voltage-gated channel subfamily H member 2 | protein | 110 | 24% helix, 40% strand | Q12809 |
Compared structures
- 4HQA · Crystal structure of PAS domain from the human ERG (hERG) potassium 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 0.97
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 Q12809
- Elsewhere: RCSB PDB 4HQA · PDBe 4HQA · UniProt Q12809
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