› 2wll

X-ray diffraction
3.65Å resolution

POTASSIUM CHANNEL FROM BURKHOLDERIA PSEUDOMALLEI

Released:
DOI: 10.2210/pdb2wll/pdb
PDB entry 2wll coloured by chain, front view.
PDB entry 2wll coloured by chain, side view.
PDB entry 2wll coloured by chain, top view.
Source organism: Burkholderia pseudomallei
Primary publication:
Domain reorientation and rotation of an intracellular assembly regulate conduction in Kir potassium channels.
Clarke OB, Caputo AT, Hill AP, Vandenberg JI, Smith BJ, Gulbis JM
Cell 141 1018-29 (2010)
PMID: 20564790

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160728 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Potassium channel Chain: A
Molecule details ›
Chain: A
Length: 333 amino acids
Theoretical weight: 37.2 KDa
Source organism: Burkholderia pseudomallei
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P83698 (Residues: 1-333; Coverage: 100%)
Gene name: Y036_1623
Sequence domains:
Structure domains:
Potassium channel Chain: B
Molecule details ›
Chain: B
Length: 333 amino acids
Theoretical weight: 37.18 KDa
Source organism: Burkholderia pseudomallei
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P83698 (Residues: 1-333; Coverage: 100%)
Gene name: Y036_1623
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MG 3 x MG
Ligand K 2 x K
Ligand PLC 2 x PLC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: I222
Unit cell:
a: 92.84Å b: 105.62Å c: 258.63Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.248 0.246 0.286
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

14 review citations

GPCR mediated regulation of synaptic transmission.
Betke et al. (2012)
13 more

10 mentions without citation

Phosphoinositide control of membrane protein function: a frontier led by studies on ion channels.
Logothetis et al. (2015)
9 more