Research workbench
Structure of the ankyrin domain of an arabidopsis thaliana potassium channel
Analyse Structure of the ankyrin domain of an arabidopsis thaliana potassium channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5AAR
- Type
- protein
- Length
- 185 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Potassium channel AKT1
- UniProt
- Q38998
- Ligands
- MG
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Potassium channel AKT1 | protein | 185 | 55% helix, 0% strand | Q38998 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5AAR · Structure of the ankyrin domain of an Arabidopsis Thaliana potassium channel · the same entry in another collection · chain A against A, TM-score 1.00
- Q38998 · AlphaFold monomer V2.0 prediction for potassium channel AKT1 (Q38998) · 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 Q38998
- Elsewhere: RCSB PDB 5AAR · PDBe 5AAR · UniProt Q38998
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