23XI: Human sodium/proton antiporter NHE1

Cryo-EM structure of human sodium/proton antiporter NHE1 in complex with Zoniporide in an outward-open conformation. Determined by electron microscopy at 2.93 Å resolution. Released 5 Aug 2026.

Method
Electron microscopy
Resolution
2.93 Å
Organism
Homo sapiens
Chains
2
Atoms
6,749
Mol. weight
184.12 kDa
Ligands
A1E6C, PS1
Released
5 Aug 2026

Explore 23XI in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

23XI contains 47 α-helices and 4 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.

Chain A: 24 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix100-12122
α-helix124-1285
α-helix131-14919
α-helix158-1603
α-helix161-1655
α-helix166-17510
α-helix179-1846
α-helix186-1905
α-helix191-1966
α-helix197-21317
α-helix224-23411
β-strand23711
α-helix239-2468
α-helix253-26412
α-helix267-28216
α-helix288-32134
α-helix330-34718
α-helix352-36918
α-helix376-40328
α-helix411-43727
α-helix446-4538
β-strand45811
α-helix460-4678
α-helix477-48913
α-helix490-4956
α-helix496-50510
Chain B: 23 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix100-12122
α-helix124-1285
α-helix131-14919
α-helix158-1603
α-helix161-1655
α-helix166-17510
α-helix179-1846
α-helix186-1905
α-helix191-1966
α-helix197-21317
α-helix224-23411
β-strand23712
α-helix239-2468
α-helix253-28230
α-helix288-32134
α-helix330-34718
α-helix352-36918
α-helix376-40328
α-helix411-43727
α-helix446-4538
β-strand45812
α-helix460-4678
α-helix477-48913
α-helix490-4956
α-helix496-50510

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Sodium/hydrogen exchanger 1A, Bprotein815Homo sapiensP19634 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>23XI_1 Sodium/hydrogen exchanger 1 (chains A, B)
MVLRSGICGLSPHRIFPSLLVVVALVGLLPVLRSHGLQLSPTASTIRSSEPPRERSIGDV
TTAPPEVTPESRPVNHSVTDHGMKPRKAFPVLGIDYTHVRTPFEISLWILLACLMKIGFH
VIPTISSIVPESCLLIVVGLLVGGLIKGVGETPPFLQSDVFFLFLLPPIILDAGYFLPLR
QFTENLGTILIFAVVGTLWNAFFLGGLMYAVCLVGGEQINNIGLLDNLLFGSIISAVDPV
AVLAVFEEIHINELLHILVFGESLLNDAVTVVLYHLFEEFANYEHVGIVDIFLGFLSFFV
VALGGVLVGVVYGVIAAFTSRFTSHIRVIEPLFVFLYSYMAYLSAELFHLSGIMALIASG
VVMRPYVEANISHKSHTTIKYFLKMWSSVSETLIFIFLGVSTVAGSHHWNWTFVISTLLF
CLIARVLGVLGLTWFINKFRIVKLTPKDQFIIAYGGLRGAIAFSLGYLLDKKHFPMCDLF
LTAIITVIFFTVFVQGMTIRPLVDLLAVKKKQETKRSINEEIHTQFLDHLLTGIEDICGH
YGHHHWKDKLNRFNKKYVKKCLIAGERSKEPQLIAFYHKMEMKQAIELVESGGMGKIPSA
VSTVSMQNIHPKSLPSERILPALSKDKEEEIRKILRNNLQKTRQRLRSYNRHTLVADPYE
EAWNQMLLRRQKARQLEQKINNYLTVPAHKLDSPTMSRARIGSDPLAYEPKEDLPVITID
PASPQSPESVDLVNEELKGKVLGLSRDPAKVAEEDEDDDGGIMMRSKETSSPGTDDVFTP
APSDSPSSQRIQRCLSDPGPHPEPGEGEPFFPKGQ

Ligands and cofactors

IDNameFormulaCopies
A1E6CZoniporideC17 H16 N6 O2
PS11,2-didecanoyl-sn-glycero-3-[phospho-L-serine]C26 H49 N O10 P3

Water and common crystallization additives (NA) are not listed.

Primary citation

Structure and transport mechanism of the human sodium/proton antiporter NHE1. Cong, Y., Kong, F., Zhu, A. et al. To be published.

Other PDB entries of the same protein (UniProt P19634 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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