› 3ogc

X-ray diffraction
3.8Å resolution

KcsA E71A variant in presence of Na+

Released:
DOI: 10.2210/pdb3ogc/pdb
PDB entry 3ogc coloured by chain, front view.
PDB entry 3ogc coloured by chain, side view.
PDB entry 3ogc coloured by chain, top view.
Source organisms:
Primary publication:
Mechanism for selectivity-inactivation coupling in KcsA potassium channels.
Cheng WW, McCoy JG, Thompson AN, Nichols CG, Nimigean CM
Proc Natl Acad Sci U S A 108 5272-7 (2011)
PMID: 21402935

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-209471 (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
Expression system: Not provided
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
Expression system: Not provided
Structure domains: Immunoglobulins
pH-gated potassium channel KcsA Chain: C
Molecule details ›
Chain: C
Length: 131 amino acids
Theoretical weight: 14.11 KDa
Source organism: Streptomyces lividans
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A334 (Residues: 2-124; Coverage: 77%)
Gene names: kcsA, skc1
Sequence domains: Ion channel
Structure domains: Helix Hairpins

Ligands and Environments

1 bound ligand:
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: I4
Unit cell:
a: 154.735Å b: 154.735Å c: 75.401Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.249 0.247 0.283
Expression systems:
  • Not provided
  • Escherichia coli

Quick links

Citations

9 review citations

Voltage-Gated Potassium Channels: A Structural Examination of Selectivity and Gating.
Kim et al. (2016)
8 more

4 mentions without citation

Structure of potassium channels.
Kuang et al. (2015)
3 more