› 6iv4

X-ray diffraction
3.14Å resolution

Crystal structure of a bacterial Bestrophin homolog from Klebsiella pneumoniae with a mutation W252F

Released:
DOI: 10.2210/pdb6iv4/pdb
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PDB entry 6iv4 coloured by chain, front view.
PDB entry 6iv4 coloured by chain, side view.
PDB entry 6iv4 coloured by chain, top view.
Source organism: Klebsiella pneumoniae IS53
Primary publication:
Dual Ca2+-dependent gates in human Bestrophin1 underlie disease-causing mechanisms of gain-of-function mutations.
Ji C, Kittredge A, Hopiavuori A, Ward N, Chen S, Fukuda Y, Zhang Y, Yang T
OpenAccess logo Commun Biol 2 240 (2019)
PMID: 31263784

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-237322 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bestrophin homolog Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 296 amino acids
Theoretical weight: 33.71 KDa
Source organism: Klebsiella pneumoniae IS53
Expression system: Escherichia coli

Ligands and Environments

1 bound ligand:
Ligand ZN 13 x ZN
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P212121
Unit cell:
a: 104.009Å b: 154.186Å c: 161.736Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.243 0.238 0.295
Expression system: Escherichia coli

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Citations

1 review citation

Structure and Function of the Bestrophin family of calcium-activated chloride channels.
Owji et al. (2021)
11 other articles

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