› 2k1e

Solution NMR

NMR studies of a channel protein without membranes: structure and dynamics of water-solubilized KcsA

Released:
DOI: 10.2210/pdb2k1e/pdb
PDB entry 2k1e coloured by chain, ensemble of 20 models, front view.
PDB entry 2k1e coloured by chain, ensemble of 20 models, side view.
PDB entry 2k1e coloured by chain, ensemble of 20 models, top view.
Source organism: Escherichia coli
Primary publication:
NMR studies of a channel protein without membranes: structure and dynamics of water-solubilized KcsA.
Ma D, Tillman TS, Tang P, Meirovitch E, Eckenhoff R, Carnini A, Xu Y
Proc Natl Acad Sci U S A 105 16537-42 (2008)
PMID: 18948596

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162803 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
water soluble analogue of potassium channel, KcsA Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 103 amino acids
Theoretical weight: 11.4 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
Structure domains: Helix Hairpins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Normal mode analysis of biomolecular structures: functional mechanisms of membrane proteins.
Bahar et al. (2010)
5 more

6 mentions without citation

Membrane proteins: always an insoluble problem?
Rawlings AE. (2016)
5 more