› 5x87

X-ray diffraction
3.14Å resolution

Crystal structure of a bacterial Bestrophin homolog from Klebsiella pneumoniae with a mutation L177T

Released:
DOI: 10.2210/pdb5x87/pdb
PDB entry 5x87 coloured by chain, front view.
PDB entry 5x87 coloured by chain, side view.
PDB entry 5x87 coloured by chain, top view.
Source organism: Klebsiella pneumoniae
Primary publication:
Patient-specific mutations impair BESTROPHIN1's essential role in mediating Ca2+-dependent Cl- currents in human RPE.
Li Y, Zhang Y, Xu Y, Kittredge A, Ward N, Chen S, Tsang SH, Yang T
Elife 6 (2017)
PMID: 29063836

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-237299 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bestrophin Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 297 amino acids
Theoretical weight: 33.82 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli

Ligands and Environments

1 bound ligand:
Ligand ZN 15 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P212121
Unit cell:
a: 114.485Å b: 160.573Å c: 162.657Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.199 0.237
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Sorsby fundus dystrophy: Insights from the past and looking to the future.
Anand-Apte et al. (2019)
2 more