5Y4O: MscS channel, YnaI

Cryo-EM structure of MscS channel, YnaI. Determined by electron microscopy at 3.8 Å resolution. Released 20 Mar 2019.

Method
Electron microscopy
Resolution
3.8 Å
Organism
Escherichia coli O157:H7
Chains
7
Atoms
12,341
Mol. weight
277.35 kDa
Released
20 Mar 2019

Explore 5Y4O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5Y4O contains 56 α-helices and 96 β-strands across 7 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chains A, B, C and D: 8 helices, 14 β-strands

ElementResiduesLengthSheet
α-helix115-13723
α-helix142-1443
α-helix145-17531
β-strand18411
β-strand19511
β-strand196-19942
β-strand204-20632
β-strand20713
β-strand21313
α-helix218-2225
α-helix229-2313
β-strand235-23844
β-strand24315
α-helix245-2506
α-helix251-26414
β-strand26814
β-strand274-27744
β-strand289-29464
α-helix299-31921
β-strand32415
β-strand32816
β-strand33017
Chain E: 8 helices, 14 β-strands
ElementResiduesLengthSheet
α-helix115-13723
α-helix142-1443
α-helix145-17531
β-strand184126
β-strand195126
β-strand196-199427
β-strand204-206327
β-strand207128
β-strand213128
α-helix218-2225
α-helix229-2313
β-strand235-238429
β-strand243130
α-helix245-2506
α-helix251-26414
β-strand268129
β-strand274-277429
β-strand289-294629
α-helix299-31921
β-strand324130
β-strand328125
β-strand330-331231
Chain F: 8 helices, 13 β-strands
ElementResiduesLengthSheet
α-helix115-13723
α-helix142-1443
α-helix145-17531
β-strand184132
β-strand195132
β-strand196-199433
β-strand204-206333
β-strand207134
β-strand213134
α-helix218-2225
α-helix229-2313
β-strand235-238435
β-strand243136
α-helix245-2506
α-helix251-26414
β-strand268135
β-strand274-277435
β-strand289-294635
α-helix299-31921
β-strand324136
β-strand328-329231
Chain G: 8 helices, 13 β-strands
ElementResiduesLengthSheet
α-helix115-13723
α-helix142-1443
α-helix145-17531
β-strand184137
β-strand195137
β-strand196-199438
β-strand204-206338
β-strand207139
β-strand213139
α-helix218-2225
α-helix229-2313
β-strand235-238440
β-strand243141
α-helix245-2506
α-helix251-26414
β-strand268140
β-strand274-277440
β-strand289-294640
α-helix299-31921
β-strand324141
β-strand33016

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Low conductance mechanosensitive channel YnaIA, B, C, D, E, F, Gprotein349Escherichia coli O157:H7P0AEB5 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F, G), FASTA
>5Y4O_1 Low conductance mechanosensitive channel YnaI (chains A, B, C, D, E, F, G)
MIAELFTNNALNLVIIFGSCAALILMSFWFRRGNRKRKGFLFHAVQFLIYTIIISAVGSI
INYVIENYKLKFITPGVIDFICTSLIAVILTIKLFLLINQFEKQQIKKGRDITSARIMSR
IIKITIIVVLVLLYGEHFGMSLSGLLTFGGIGGLAVGMAGKDILSNFFSGIMLYFDRPFS
IGDWIRSPDRNIEGTVAEIGWRITKITTFDNRPLYVPNSLFSSISVENPGRMTNRRITTT
IGLRYEDAAKVGVIVEAVREMLKNHPAIDQRQTLLVYFNQFADSSLNIMVYCFTKTTVWA
EWLAAQQDVYLKIIDIVQSHGADFAFPSQTLYMDNITPPEQGRHHHHHH

Primary citation

A binding-block ion selective mechanism revealed by a Na/K selective channel. Yu, J., Zhang, B., Zhang, Y. et al. Protein Cell (2018) 9:629-639. DOI 10.1007/s13238-017-0465-8 · PubMed

Other PDB entries of the same protein (UniProt P0AEB5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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