› 5e1a

X-ray diffraction
3.4Å resolution

Structure of KcsA with L24C/R117C mutations

Released:
DOI: 10.2210/pdb5e1a/pdb
PDB entry 5e1a coloured by chain, front view.
PDB entry 5e1a coloured by chain, side view.
PDB entry 5e1a coloured by chain, top view.
Source organisms:
Primary publication:
Conformational heterogeneity in closed and open states of the KcsA potassium channel in lipid bicelles.
Kim DM, Dikiy I, Upadhyay V, Posson DJ, Eliezer D, Nimigean CM
J Gen Physiol 148 119-32 (2016)
PMID: 27432996

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero dimer
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141094 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
antibody Fab fragment heavy chain Chain: A
Molecule details ›
Chain: A
Length: 219 amino acids
Theoretical weight: 23.41 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins
antibody Fab fragment light chain Chain: B
Molecule details ›
Chain: B
Length: 212 amino acids
Theoretical weight: 23.44 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins
pH-gated potassium channel KcsA Chain: C
Molecule details ›
Chain: C
Length: 124 amino acids
Theoretical weight: 13.16 KDa
Source organism: Streptomyces lividans
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A334 (Residues: 4-124; Coverage: 76%)
Gene names: kcsA, skc1
Sequence domains: Ion channel
Structure domains: Helix Hairpins

Ligands and Environments

1 bound ligand:
Ligand K 4 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: I4
Unit cell:
a: 154.794Å b: 154.794Å c: 74.479Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.248 0.247 0.257
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Spotlight on the Ballet of Proteins: The Structural Dynamic Properties of Proteins Illuminated by Solution NMR.
Tokunaga et al. (2020)
11 other articles

1 mention without citation

Conformational heterogeneity in closed and open states of the KcsA potassium channel in lipid bicelles.
Kim et al. (2016)