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6IV2

Crystal structure of a bacterial Bestrophin homolog from Klebsiella pneumoniae with a mutation Y211A

Summary for 6IV2
Entry DOI10.2210/pdb6iv2/pdb
Related4wd8
DescriptorBestrophin homolog, ZINC ION (3 entities in total)
Functional Keywordsbestrophin-1, homolog, mutation, klebsiella pneumoniae, membrane protein
Biological sourceKlebsiella pneumoniae IS53
Total number of polymer chains5
Total formula weight169045.26
Authors
Kittredge, A.,Chen, S.,Yang, T. (deposition date: 2018-12-02, release date: 2019-11-13, Last modification date: 2022-06-08)
Primary citationJi, C.,Kittredge, A.,Hopiavuori, A.,Ward, N.,Chen, S.,Fukuda, Y.,Zhang, Y.,Yang, T.
Dual Ca2+-dependent gates in human Bestrophin1 underlie disease-causing mechanisms of gain-of-function mutations.
Commun Biol, 2:240-240, 2019
Cited by
PubMed: 31263784
DOI: 10.1038/s42003-019-0433-3
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.62 Å)
Structure validation

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