Cryo-EM structure of Sodium proton exchanger NhaA with bound cardiolipin. Determined by electron microscopy at 3.37 Å resolution. Released 21 Feb 2024.
Explore 8PS0 in 3D Show helices and sheets RCSB PDB PDBe
8PS0 contains 41 α-helices and 10 β-strands across 2 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 15-28 | 14 | |
| β-strand | 31 | 1 | 1 |
| β-strand | 33 | 1 | 1 |
| β-strand | 45-50 | 6 | 2 |
| β-strand | 53-58 | 6 | 2 |
| α-helix | 59-84 | 26 | |
| α-helix | 95-104 | 10 | |
| α-helix | 107-112 | 6 | |
| α-helix | 113-115 | 3 | |
| α-helix | 120-123 | 4 | |
| α-helix | 135-142 | 8 | |
| α-helix | 150-173 | 24 | |
| α-helix | 181-200 | 20 | |
| α-helix | 205-218 | 14 | |
| α-helix | 224-234 | 11 | |
| β-strand | 242 | 1 | 3 |
| β-strand | 245 | 1 | 3 |
| α-helix | 247-258 | 12 | |
| α-helix | 259-263 | 5 | |
| α-helix | 287-294 | 8 | |
| α-helix | 295-299 | 5 | |
| α-helix | 300-311 | 12 | |
| α-helix | 319-320 | 2 | |
| α-helix | 325-334 | 10 | |
| α-helix | 339-349 | 11 | |
| α-helix | 355-378 | 24 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 16-30 | 15 | |
| α-helix | 35-41 | 7 | |
| β-strand | 45-49 | 5 | 2 |
| β-strand | 55-58 | 4 | 2 |
| α-helix | 59-85 | 27 | |
| α-helix | 95-104 | 10 | |
| α-helix | 107-116 | 10 | |
| α-helix | 122-125 | 4 | |
| α-helix | 135-143 | 9 | |
| α-helix | 150-173 | 24 | |
| α-helix | 181-200 | 20 | |
| α-helix | 205-218 | 14 | |
| α-helix | 223-236 | 14 | |
| β-strand | 242 | 1 | 4 |
| β-strand | 245 | 1 | 4 |
| α-helix | 247-258 | 12 | |
| α-helix | 259-263 | 5 | |
| α-helix | 264-270 | 7 | |
| α-helix | 281-284 | 4 | |
| α-helix | 288-293 | 6 | |
| α-helix | 294-299 | 6 | |
| α-helix | 300-313 | 14 | |
| α-helix | 326-335 | 10 | |
| α-helix | 339-349 | 11 | |
| α-helix | 355-379 | 25 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Na(+)/H(+) antiporter NhaA | A, B | protein | 396 | Escherichia coli | P13738 (AlphaFold model) |
>8PS0_1 Na(+)/H(+) antiporter NhaA (chains A, B) MKHLHRFFSSDASGGIILIIAAILAMIMANSGATSGWYHDFLETPVQLRVGSLEINKNML LWINDALMAVFFLLVGLEVKRELMQGSLASLRQAAFPVIAAIGGMIVPTLLYLAFNYADP ITREGWAIPAATDIAFALGVLALLGSRVPLALKIFLMALAIIDDLGAIIIIALFYTNDLS MASLGVAAVAIAVLAVLNLCGARRTGVYILVGVVLWTAVLKSGVHATLAGVIVGFFIPLK EKHGRSPAKRLEHVLHPWVAYLILPLFAFANAGVSLGGVTLDGLTSILPLGIIAGMLIGK PLGISLFCWLALRLKLAHLPEGTTYQQIMVVGILCGIGFTMSIFIASLAFGSVDPELINW AKLGILVGSISSAVIGYSWLRVRLRPSVGSENLYFQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| CDL | Cardiolipin | C81 H156 O17 P2 | 3 |
PIP 2 -mediated oligomerization of the endosomal sodium/proton exchanger NHE9. Kokane, S., Gulati, A., Meier, P.F. et al. Nat Commun (2025) 16:3055-3055. DOI 10.1038/s41467-025-58247-x · PubMed
Other PDB entries of the same protein (UniProt P13738 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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