Research workbench
Open mthk pore structure soaked in 10 mm BA2+/100 mm K+
Analyse Open mthk pore structure soaked in 10 mm BA2+/100 mm K+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QE9
- Type
- protein
- Length
- 83 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calcium-gated potassium channel mthk
- UniProt
- O27564
- Ligands
- K
Structure
x-ray diffraction · 1 distinct chain · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calcium-gated potassium channel mthk | protein | 83 | 78% helix, 0% strand | O27564 |
Ligands and binding sites
- K · Potassium ion · metal · 6 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4QE9 · Open MthK pore structure soaked in 10 mM Ba2+/100 mM K+ · the same entry in another collection · chain A against A, TM-score 1.00
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 O27564
- Elsewhere: RCSB PDB 4QE9 · PDBe 4QE9 · UniProt O27564
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