Cryo-EM structure of the consensus inward-facing apo NhaA dimer at pH 7.5. Determined by electron microscopy at 2.7 Å resolution. Released 17 Jun 2026.
Explore 9RH1 in 3D Show helices and sheets RCSB PDB PDBe
9RH1 contains 56 α-helices and 56 β-strands across 6 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 | 13-30 | 18 | |
| α-helix | 32-42 | 11 | |
| β-strand | 45-50 | 6 | 1 |
| β-strand | 53-58 | 6 | 1 |
| α-helix | 59-84 | 26 | |
| α-helix | 91-116 | 26 | |
| α-helix | 122-125 | 4 | |
| α-helix | 128-130 | 3 | |
| α-helix | 134-142 | 9 | |
| α-helix | 145-147 | 3 | |
| α-helix | 150-174 | 25 | |
| α-helix | 181-199 | 19 | |
| α-helix | 205-218 | 14 | |
| α-helix | 223-236 | 14 | |
| β-strand | 242 | 1 | 2 |
| β-strand | 245 | 1 | 2 |
| α-helix | 247-258 | 12 | |
| α-helix | 259-263 | 5 | |
| α-helix | 264-271 | 8 | |
| α-helix | 283-285 | 3 | |
| α-helix | 287-293 | 7 | |
| α-helix | 294-299 | 6 | |
| α-helix | 300-313 | 14 | |
| α-helix | 325-334 | 10 | |
| α-helix | 339-350 | 12 | |
| α-helix | 355-383 | 29 | |
| α-helix | 385-386 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 3 |
| β-strand | 10-12 | 3 | 4 |
| β-strand | 18-25 | 8 | 3 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-40 | 7 | 4 |
| β-strand | 44-51 | 8 | 4 |
| β-strand | 58-60 | 3 | 4 |
| β-strand | 65 | 1 | 3 |
| β-strand | 68-73 | 6 | 3 |
| β-strand | 78-83 | 6 | 3 |
| β-strand | 92-99 | 8 | 4 |
| α-helix | 100 | 1 | |
| β-strand | 105-108 | 4 | 4 |
| β-strand | 112-116 | 5 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-6 | 3 | 5 |
| β-strand | 10-12 | 3 | 6 |
| β-strand | 19-20 | 2 | 5 |
| β-strand | 23-25 | 3 | 5 |
| β-strand | 33-38 | 6 | 6 |
| β-strand | 44-49 | 6 | 6 |
| β-strand | 53-54 | 2 | 6 |
| α-helix | 55 | 1 | |
| β-strand | 62-66 | 5 | 5 |
| β-strand | 70-75 | 6 | 5 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-90 | 6 | 6 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 6 |
| β-strand | 102-105 | 4 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-5 | 2 | 10 |
| β-strand | 10-12 | 3 | 11 |
| β-strand | 19-20 | 2 | 10 |
| β-strand | 23-25 | 3 | 10 |
| β-strand | 33-38 | 6 | 11 |
| β-strand | 44-49 | 6 | 11 |
| β-strand | 53-54 | 2 | 11 |
| α-helix | 55 | 1 | |
| β-strand | 62-66 | 5 | 10 |
| β-strand | 70-75 | 6 | 10 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-90 | 6 | 11 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 11 |
| β-strand | 102-105 | 4 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Na(+)/H(+) antiporter NhaA | A, D | protein | 407 | Escherichia coli | P13738 (AlphaFold model) |
| Fv6F9 heavy chain | B, E | protein | 127 | Mus musculus | |
| Fv6F9 light chain | C, F | protein | 119 | Mus musculus |
>9RH1_1 Na(+)/H(+) antiporter NhaA (chains A, D) MKHLHRFFSSDASGGIILIIAAILAMIMANSGATSGWYHDFLETPVQLRVGSLEINKNML LWINDALMAVFFLLVGLEVKRELMQGSLASLRQAAFPVIAAIGGMIVPALLYLAFNYADP ITREGWAIPAATDIAFALGVLALLGSRVPLALKIFLMALAIIDDLGAIIIIALFYTNDLS MASLGVAAVAIAVLAVLNLCGARRTGVYILVGVVLWTAVLKSGVHATLAGVIVGFFIPLK EKHGRSPAKRLEHVLHPWVAYLILPLFAFANAGVSLQGVTLDGLTSILPLGIIAGLLIGK PLGISLFCWLALRLKLAHLPEGTTYQQIMVVGILCGIGFTMSIFIASLAFGSVDPELINW AKLGILVGSISSAVIGYSWLRVRLRPSVAAAIEGRIEGRLEHHHHHH
>9RH1_2 Fv6F9 heavy chain (chains B, E) EVKLHQSGAELVRPGASVKLSCKALGYTFSDYEMHWVKQTPVHGLEWIGAIHPGSGGTAY NQKFKGKATLTADKSSSTAYMELSSLTSEDPAVYYCTKEEYGNDFDYWGQGTTVTVSSAW RHPQFGG
>9RH1_3 Fv6F9 light chain (chains C, F) DIELTQTPSSLSASLGERVSLTCRASQEISGYLSWLQQKPDGTIKRLIYAASTLDSGVPK RFSGSRSGSDYSLTISSLESEDFADYYCLQYASYPFTFGSGTKLEIKREQKLISEEDLN
| ID | Name | Formula | Copies |
|---|---|---|---|
| CDL | Cardiolipin | C81 H156 O17 P2 | 1 |
| PGT | (1S)-2-{[{[(2R)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(palmitoylo… | C40 H79 O10 P | 1 |
pH-dependent activation of the Na + /H + antiporter NhaA and conformational dynamics of its N-terminus. Weng, T.H., Fabian, B., Olkhova, E. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-73424-2 · 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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