4RAX: A regulatory domain of an ion channel

A regulatory domain of an ion channel. Determined by X-ray diffraction at 1.45 Å resolution. Released 23 Sept 2015.

Method
X-ray diffraction
Resolution
1.45 Å
Organism
Mus musculus
Chains
1
Atoms
2,159
Mol. weight
28.35 kDa
Released
23 Sept 2015

Explore 4RAX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4RAX contains 10 α-helices and 16 β-strands across 1 chain. 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.

Chain A: 10 helices, 16 β-strands

ElementResiduesLengthSheet
β-strand221911
β-strand2225-223282
α-helix2236-22372
β-strand2239-224352
β-strand2248-225033
α-helix2251-22522
α-helix2253-226311
α-helix2267-22737
α-helix2278-22803
β-strand2281-228773
β-strand228914
α-helix2298-231013
β-strand2315-2324102
α-helix2327-23293
β-strand2335-2344102
α-helix2349-23579
β-strand2366-237274
β-strand2375-237843
β-strand238312
β-strand238613
α-helix2394-23974
β-strand2399-2409114
β-strand2426-243494
β-strand2443-245083
β-strand245311
α-helix2454-24563

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Piezo-type mechanosensitive ion channel component 1Aprotein252Mus musculusE2JF22 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4RAX_1 Piezo-type mechanosensitive ion channel component 1 (chains A)
RSVVGVVNQPIDVTVTLKLGGYEPLFTMSAQQPSIVPFTPQAYEELSQQFDPYPLAMQFI
SQYSPEDIVTAQIEGSSGALWRISPPSRAQMKQELYNGTADITLRFTWNFQRDLAKGGTV
EYTNEKHTLELAPNSTARRQLAQLLEGRPDQSVVIPHLFPKYIRAPNGPEANPVKQLQPD
EEEDYLGVRIQLRREQVGTGASGEQAGTKASDFLEWWVIELQDCKADCNLLPMVIFSDKV
SPPSVEHHHHHH

Primary citation

Architecture of the mammalian mechanosensitive Piezo1 channel. Ge, J., Li, W., Zhao, Q. et al. Nature (2015) 527:64-69. DOI 10.1038/nature15247 · PubMed

Other PDB entries of the same protein (UniProt E2JF22 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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