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› 6ivr

X-ray diffraction
2.8Å resolution

Crystal structure of a membrane protein W16A

Released:
DOI: 10.2210/pdb6ivr/pdb
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PDB entry 6ivr coloured by chain, front view.
PDB entry 6ivr coloured by chain, side view.
PDB entry 6ivr coloured by chain, top view.
Source organism: Klebsiella pneumoniae
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:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-237479 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Predicted membrane protein Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 297 amino acids
Theoretical weight: 33.72 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: W9BH30 (Residues: 1-294; Coverage: 96%)
Gene names: B5L96_30355, BANRA_02438, BANRA_04102, BL124_00003590, CP554_21535, DM078_14870, DW286_05495, E1814_02345, EA160_26845, EAO17_00845, EAO28_28340, EXT45_12770, FXN67_01795, GJJ01_10895, GJJ08_012945, GJJ18_05220, GNF00_19285, H3G96_014970, JMZ77_12400, LS45_10030, NCTC11679_02573, NCTC13465_00112, NCTC5051_02566, NCTC5052_01714, NCTC8849_03195, NCTC9637_03467, NCTC9645_05950, Q6294_11555, SAMEA104567804_03846, SAMEA2273558_01246, SAMEA3499874_04755, SAMEA3649591_04364, SAMEA3720909_04618, SAMEA3729652_00264
Sequence domains: Bestrophin, RFP-TM, chloride channel

Ligands and Environments

4 bound ligands:
Ligand ZN 15 x ZN
Ligand EDO 1 x EDO
Ligand CL 11 x CL
Ligand ACY 2 x ACY
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P212121
Unit cell:
a: 113.914Å b: 159.568Å c: 161.724Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.217 0.248
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

PDB-REDO

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