› 3hpl

X-ray diffraction
3.2Å resolution

KcsA E71H-F103A mutant in the closed state

Released:
DOI: 10.2210/pdb3hpl/pdb
PDB entry 3hpl coloured by chain, front view.
PDB entry 3hpl coloured by chain, side view.
PDB entry 3hpl coloured by chain, top view.
Source organisms:
Primary publication:
Structural basis for the coupling between activation and inactivation gates in K(+) channels.
Cuello LG, Jogini V, Cortes DM, Pan AC, Gagnon DG, Dalmas O, Cordero-Morales JF, Chakrapani S, Roux B, Perozo E
Nature 466 272-5 (2010)
PMID: 20613845

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-209447 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Antibody Fab 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 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: 124 amino acids
Theoretical weight: 13.14 KDa
Source organism: Streptomyces lividans
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A334 (Residues: 1-124; Coverage: 78%)
Gene names: kcsA, skc1
Sequence domains: Ion channel
Structure domains: Helix Hairpins

Ligands and Environments

1 bound ligand:
Ligand K 6 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: I4
Unit cell:
a: 156.14Å b: 156.14Å c: 76.292Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.22 0.269
Expression systems:
  • Not provided
  • Escherichia coli

Quick links

Citations

32 review citations

hERG K(+) channels: structure, function, and clinical significance.
Vandenberg et al. (2012)
31 more

1 mention without citation

Structural basis for the coupling between activation and inactivation gates in K(+) channels.
Cuello et al. (2010)