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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：P19634 New Search
19PDB entries
19Biological assembly
26chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
1Y4E NMR structure of transmembrane segment IV of the NHE1 isoform of the Na+/H+ exchanger Deposited 2004-11-30 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 155–180（26 aa） Fragment：Transmembrane segment IV
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions 303 K；Pressure ambient
NMR sample composition 2 mM TM IV, unlabelled; 1 mM DSS, CDCl3:CD3OH:H2O (4:4:1 v:v:v) | CDCl3:CD3OH:H2O (4:4:1 v:v:v)
NMR sample composition 2 mM TM IV, U-15N; 1 mM DSS, CDCl3:CD3OH:H2O (4:4:1 v:v:v) | CDCl3:CD3OH:H2O (4:4:1 v:v:v)
Resolution not provided
23XK Cryo-EM structure of human sodium/proton antiporter NHE1 in complex with Cariporide in an outward-open conformation Deposited 2026-02-24 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–815（815 aa）
Chain B 1–815（815 aa）
Not recorded HG0 N-[bis(azanyl)methylidene]-3-methylsulfonyl-4-propan-2-yl-benzamide × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.10 Å
23XM Cryo-EM structure of human sodium/proton antiporter NHE1 in complex with Eniporide in an outward-open conformation Deposited 2026-02-24 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–815（815 aa）
Chain B 1–815（815 aa）
Not recorded A1E6D Eniporide × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.24 Å
23XO Cryo-EM structure of human sodium/proton antiporter NHE1 in complex with Rimeporide in an outward-open conformation Deposited 2026-02-24 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–815（815 aa）
Chain B 1–815（815 aa）
Not recorded A1E6E ~{N}-carbamimidoyl-2-methyl-4,5-bis(methylsulfonyl)benzamide × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.16 Å
2BEC Crystal structure of CHP2 in complex with its binding region in NHE1 and insights into the mechanism of pH regulation Deposited 2005-10-24 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 503–545（43 aa） Fragment：residues 503-545
Not recorded YT3 YTTRIUM (III) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；25% PEG 3350, 0.2M ammonium acetate, 0.1M Bis-Tris, 0.01M yttrium chloride, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.70 Å R-free 0.287
2E30 Solution structure of the cytoplasmic region of Na+/H+ exchanger 1 complexed with essential cofactor calcineurin B homologous protein 1 Deposited 2006-11-19 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 503–545（43 aa） Fragment：NHE1 fragment (503-545)
Not recorded CA CALCIUM ION × 2 SOLUTION NMR
NMR measurement conditions pH 6.9；310 K；Ionic strength (raw mmCIF value) 30mM；Pressure ambient
NMR sample composition 0.9mM CHP1/NHE1 U-15N, U-13C, 50mM Tris buffer, 99% D2O | 99% D2O
NMR sample composition 0.5mM CHP1/NHE1 60%2H, U-15N, U-13C, 50mM Tris buffer, 95% H2O, 5% D2O | 95% H2O/5% D2O
NMR sample composition 0.9mM CHP1/NHE1 U-15N, 50mM Tris buffer, 95% H2Om, 5% D2O | 95% H2O/5% D2O
NMR sample composition 0.9mM CHP1/NHE1 U-15N, U-13C, 50mM Tris buffer, 95% H2O, 5% D2O | 95% H2O/5% D2O
NMR sample composition 0.5mM CHP1/NHE1 U-15N, 15%-13C, 50mM Tris buffer, 95% H2O, 5% D2O | 95% H2O/5% D2O
Resolution not provided
2HTG Structural and functional characterization of TM VII of the NHE1 isoform of the Na+/H+ exchanger Deposited 2006-07-25 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 250–274（25 aa） Fragment：Transmembrane segment VII
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 4.8；303 K；Ionic strength (raw mmCIF value) ~ 75 mM Na+/DPC-；Pressure ambient
NMR sample composition ~ 1 mM peptide synthetic source 1 (unlabeled), 90% H2O/10% D2O, ~ 75 mM dodecylphosphocholine, 1.0 mM DSS | 90% H2O/10% D2O
NMR sample composition ~ 1 mM peptide synthetic source 2 (6 specific 15N labels), 90% H2O/10% D2O, ~ 75 mM dodecylphosphocholine, 1.0 mM DSS | 90% H2O/10% D2O
Resolution not provided
2KBV Structural and functional analysis of TM XI of the NHE1 isoform of thE NA+/H+ exchanger Deposited 2008-12-09 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 447–472（26 aa） Fragment：NHE1 transmembrane segment XI
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5；303 K；Pressure ambient
NMR sample composition 150 mM DPC-1, 0.25 mM DSS-2, 2 mM TMXI-3, 95% H2O/5% D2O | 95% H2O/5% D2O
Resolution not provided
2L0E Structural and functional analysis of tm vi of the nhe1 isoform of the na+/h+ exchanger Deposited 2010-07-01 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 226–250（25 aa） Fragment：transmembrane segment VI of NHE1, UNP residues 226-250
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5；303 K；Ionic strength (raw mmCIF value) 0；Pressure ambient
NMR sample composition 2 mM TM VI-1, 0.25 mM DSS-2, 150 mM [U-2H] DPC-3, 95% H2O/5% D2O | 95% H2O/5% D2O
Resolution not provided
2MDF NMR structure of a two-transmembrane segment TM VI-VII of NHE1 Deposited 2013-09-10 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 226–274（49 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5；303 K；Ionic strength (raw mmCIF value) 0；Pressure ambient
NMR sample composition 1-2 mM [U-15N] entity, 5 % [U-2H] D2O, 0.25 mM [1,1,2,2,3,3-2H6] DSS, 95 % H2O, 75-150 mM [U-2H] dodecylphosphocholine, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 1-2 mM [U-15N] entity, 100 % [U-2H] D2O, 0.25 mM [1,1,2,2,3,3-2H6] DSS, 75-150 mM [U-2H] dodecylphosphocholine, 100% D2O | 100% D2O
Resolution not provided
2YGG Complex of CaMBR and CaM Deposited 2011-04-15 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 622–689（68 aa） Fragment：CAM BINDING REGION, RESIDUES 622-689
Not recorded MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 TAM TRIS(HYDROXYETHYL)AMINOMETHANE × 3 CA CALCIUM ION × 4 MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.23 Å R-free 0.232
6NUC Structure of Calcineurin in complex with NHE1 peptide Deposited 2019-01-31 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain C 679–723（45 aa）
Not recorded FE FE (III) ION × 1 ZN ZINC ION × 1 PO4 PHOSPHATE ION × 1 PEG DI(HYDROXYETHYL)ETHER × 1 NA SODIUM ION × 1 CA CALCIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9.5；298 K；40% (v/v) PEG 600, 100 mM CHES/ Sodium hydroxide pH 9.5, 0.2 M MgCl2
Resolution 1.90 Å R-free 0.194
6NUF Structure of Calcineurin in complex with NHE1 peptide Deposited 2019-01-31 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain C 679–723（45 aa）
Mutation：R698A, R700A FE FE (III) ION × 1 ZN ZINC ION × 1 PO4 PHOSPHATE ION × 1 PGE TRIETHYLENE GLYCOL × 2 PEG DI(HYDROXYETHYL)ETHER × 1 NA SODIUM ION × 1 CA CALCIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；40% (v/v) PEG 600, 100 mM CHES/ Sodium hydroxide pH 9.5, 0.2 M MgCl2
Resolution 1.90 Å R-free 0.209
6NUU Structure of Calcineurin mutant in complex with NHE1 peptide Deposited 2019-02-02 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain C 679–723（45 aa）
Not recorded FE FE (III) ION × 1 ZN ZINC ION × 1 PO4 PHOSPHATE ION × 1 PEG DI(HYDROXYETHYL)ETHER × 1 CA CALCIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9.5；298 K；40% (v/v) PEG 600, 100 mM CHES/ Sodium hydroxide pH 9.5, 0.2 M MgCl2
Resolution 2.30 Å R-free 0.243
6ZBI Ternary complex of Calmodulin bound to 2 molecules of NHE1 Deposited 2020-06-08 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain B 622–657（36 aa）
Chain C 622–657（36 aa）
Not recorded CA CALCIUM ION × 4 SOLUTION NMR
NMR measurement conditions pH 7.5；310 K；Ionic strength (raw mmCIF value) 120；Pressure 1
NMR sample composition 0.5 mM [U-99% 13C; U-99% 15N] Calmodulin, 1.15 mM Sodium/Hydrogen exchanger 1 (NHE1, SLC9A1), 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 1 mM [U-99% 13C; U-99% 15N] Sodium/Hydrogen exchanger 1 (NHE1, SLC9A1), 0.5 mM Calmodulin, 95% H2O/5% D2O | 95% H2O/5% D2O
Resolution not provided
7DSV Structure of a human NHE1-CHP1 complex under pH 6.5 Deposited 2021-01-03 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 87–558（472 aa）
Chain B 87–558（472 aa）
Not recorded LBN 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine × 16 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
7DSW Structure of a human NHE1-CHP1 complex under pH 7.5 Deposited 2021-01-03 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 87–506（420 aa）
Chain B 87–506（420 aa）
Not recorded LBN 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine × 12 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
7DSX Structure of a human NHE1-CHP1 complex under pH 7.5, bound by cariporide Deposited 2021-01-03 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 85–593（509 aa）
Chain B 85–593（509 aa）
Not recorded PGT (1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE × 6 HG0 N-[bis(azanyl)methylidene]-3-methylsulfonyl-4-propan-2-yl-benzamide × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.50 Å
9NXE Crystal Structure of Calcineurin Clinical Variant E282K Deposited 2025-03-25 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain C 679–723（45 aa）
Not recorded PEG DI(HYDROXYETHYL)ETHER × 1 FE FE (III) ION × 1 ZN ZINC ION × 1 CA CALCIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9；290 K；0.1 M CAPS pH 9, 0.2 M MgCl2 and 24% PEG 600
Resolution 2.09 Å R-free 0.243

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.