6nuf

Structure of Calcineurin in complex with NHE1 peptide

Method: X-RAY DIFFRACTION D_max: 102.0 Å Quality: GOOD

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform

Homo sapiens

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain A； UniProt 1–370	Not recorded	Calcineurin subunit B type 1 × 1 （P63098） Sodium/hydrogen exchanger 1 × 1 （P19634） 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

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 6NUF	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1AUI HUMAN CALCINEURIN HETERODIMER Deposited 1997-08-27	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–521（521 aa）	Not recorded	ZN ZINC ION × 1 FE FE (III) ION × 1 CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；PROTEIN WAS CRYSTALLIZED FROM 8% PEG 6000, 0.1M CACL2, 0.1M TES PH 7.5, 1 MM DTT.	Resolution 2.10 Å
1M63 Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes Deposited 2002-07-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–372（372 aa） Fragment：RESIDUES 1-372 Chain E 1–372（372 aa） Fragment：RESIDUES 1-372	Not recorded	ZN ZINC ION × 2 FE FE (III) ION × 2 CA CALCIUM ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；0.1 M NA CACODYLATE, 0.2 M MGCL2, 13% PEG8000, 2.5% ETHANOL, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K	Resolution 2.80 Å R-free 0.322
1MF8 Crystal Structure of human calcineurin complexed with cyclosporin A and human cyclophilin Deposited 2002-08-09	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 20–392（373 aa） Fragment：TRUNCATED FORM (RESIDUES 20-392)	Not recorded	PO4 PHOSPHATE ION × 1 CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；12% PEG 4000, 5MM POTASSIUM PHOSPHATE, 75MM SODIUM CITRATE, 15% GLYCEROL, 5MM TRIS, PH 4.6, MICROBATCH, TEMPERATURE 292K	Resolution 3.10 Å R-free 0.300
2JOG Structure of the calcineurin-NFAT complex Deposited 2007-03-10	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 21–347（327 aa） Fragment：residues 21-347	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.8；298 K；Ionic strength (raw mmCIF value) 0.1；Pressure ambient NMR sample composition 500uM [U-13C; U-15N; U-2H] calcineurin, 0.4-0.6 mM NFAT, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 300uM calcineurin, 0.3 mM [U-13C; U-15N; U-2H] NFAT, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 400uM [2H, FIMY-1H] calcineurin, 0.4 mM [ul-2H15N, Id1LdVg -1H13C] NFAT, 100% D2O \| 100% D2O	Resolution not provided
2JZI Structure of Calmodulin complexed with the Calmodulin Binding Domain of Calcineurin Deposited 2008-01-09	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 391–414（24 aa） Fragment：UNP residues 391-414, Calmodulin_binding_domain_of_Calcineurin	Not recorded	CA CALCIUM ION × 4	SOLUTION NMR NMR measurement conditions pH 6.5；310 K NMR sample composition 1 mM [U-99% 13C; U-99% 15N] Calmodulin, 1 mM [U-99% 13C; U-99% 15N] Calmodulin binding domain of Calcineurin, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2P6B Crystal Structure of Human Calcineurin in Complex with PVIVIT Peptide Deposited 2007-03-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–380（380 aa） Fragment：Residues 1-381 Chain C 1–380（380 aa） Fragment：Residues 1-381	Not recorded	ZN ZINC ION × 2 FE FE (III) ION × 2 PO4 PHOSPHATE ION × 2 CA CALCIUM ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；295 K；12% PEG 4000, 0.1M calcium chloride, 0.1M TES, 0.001M DTT, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.30 Å R-free 0.254
2R28 The complex Structure of Calmodulin Bound to a Calcineurin Peptide Deposited 2007-08-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 389–413（25 aa） Chain D 389–413（25 aa）	Not recorded	CA CALCIUM ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；298 K；20% PEG 3350, 0.2M ammonium phosphate, 0.1M citrite acid , pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 1.86 Å R-free 0.280
2W73 High-resolution structure of the complex between calmodulin and a peptide from calcineurin A Deposited 2008-12-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain K 395–411（17 aa） Fragment：CALMODULIN BINDING DOMAIN, RESIDUES 385-411 Chain L 395–411（17 aa） Fragment：CALMODULIN BINDING DOMAIN, RESIDUES 385-411	Not recorded	CA CALCIUM ION × 11	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.45 Å R-free 0.217
2W73 High-resolution structure of the complex between calmodulin and a peptide from calcineurin A Deposited 2008-12-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain M 395–411（17 aa） Fragment：CALMODULIN BINDING DOMAIN, RESIDUES 385-411 Chain O 395–411（17 aa） Fragment：CALMODULIN BINDING DOMAIN, RESIDUES 385-411	Not recorded	CA CALCIUM ION × 9	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.45 Å R-free 0.217
3LL8 Crystal Structure of Calcineurin in Complex with AKAP79 Peptide Deposited 2010-01-28	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 14–370（357 aa） Fragment：UNP residues 14-370	Not recorded	PO4 PHOSPHATE ION × 1 ZN ZINC ION × 1 FE FE (III) ION × 1 CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；PEG 20,000 MgSO4 CaCl2, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.00 Å R-free 0.228
3LL8 Crystal Structure of Calcineurin in Complex with AKAP79 Peptide Deposited 2010-01-28	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 14–370（357 aa） Fragment：UNP residues 14-370	Not recorded	PO4 PHOSPHATE ION × 1 ZN ZINC ION × 1 FE FE (III) ION × 1 CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；PEG 20,000 MgSO4 CaCl2, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.00 Å R-free 0.228
3LL8 Crystal Structure of Calcineurin in Complex with AKAP79 Peptide Deposited 2010-01-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 14–370（357 aa） Fragment：UNP residues 14-370 Chain C 14–370（357 aa） Fragment：UNP residues 14-370	Not recorded	PO4 PHOSPHATE ION × 2 ZN ZINC ION × 2 FE FE (III) ION × 2 CA CALCIUM ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；PEG 20,000 MgSO4 CaCl2, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.00 Å R-free 0.228
4F0Z Crystal Structure of Calcineurin in Complex with the Calcineurin-Inhibiting Domain of the African Swine Fever Virus Protein A238L Deposited 2012-05-05	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–370（370 aa） Fragment：Calcineurin A Subunit	Not recorded	GOL GLYCEROL × 8 CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；295 K；0.16 M ammonium citrate dibasic, 20% (w/v) PEG3350, VAPOR DIFFUSION, SITTING DROP, temperature 295K	Resolution 1.70 Å R-free 0.178
4Q5U Structure of calmodulin bound to its recognition site from calcineurin Deposited 2014-04-17	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 391–414（24 aa） Fragment：calmodulin-binding domain (UNP residues 391-414)	Not recorded	CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；3:1 10 mg/ml protein to mother liquor (24% PEG1000, 20% glycerol), final volume 200 nL, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 1.95 Å R-free 0.248
5C1V CRYSTAL STRUCTURE ANALYSIS OF CATALYTIC SUBUNIT OF HUMAN CALCINEURIN Deposited 2015-06-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–346（345 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 2-347	Mutation：YES	FE FE (III) ION × 1 ZN ZINC ION × 1 PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；290 K；0.1 M HEPES, 25% PEG 3350, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K	Resolution 3.35 Å R-free 0.249
5C1V CRYSTAL STRUCTURE ANALYSIS OF CATALYTIC SUBUNIT OF HUMAN CALCINEURIN Deposited 2015-06-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–346（345 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 2-347	Mutation：YES	FE FE (III) ION × 1 ZN ZINC ION × 1 PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；290 K；0.1 M HEPES, 25% PEG 3350, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K	Resolution 3.35 Å R-free 0.249
5SVE Structure of Calcineurin in complex with NFATc1 LxVP peptide Deposited 2016-08-05	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–370（370 aa）	Not recorded	FE FE (III) ION × 1 ZN ZINC ION × 1 CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；0.1 M HEPES pH 7.0 15% Peg 4000	Resolution 2.60 Å R-free 0.239
6NUC Structure of Calcineurin in complex with NHE1 peptide Deposited 2019-01-31	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–370（370 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
6NUU Structure of Calcineurin mutant in complex with NHE1 peptide Deposited 2019-02-02	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–370（370 aa）	Mutation：H155A, Y159A	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
6UUQ Structure of Calcineurin bound to RCAN1 Deposited 2019-10-31	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 26–339（314 aa）	Not recorded	PO4 PHOSPHATE ION × 2 ZN ZINC ION × 1 FE FE (III) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；0.1 M Sodium cacodylate, 12% Peg 8000, 0.1 M Calcium acetate	Resolution 1.85 Å R-free 0.205
9B9G Structure of the PI4KA complex bound to Calcineurin Deposited 2024-04-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain I 2–391（390 aa） Chain I 162–391（230 aa） Chain K 2–391（390 aa） Chain K 162–391（230 aa）	Mutation：L236P,D238N Mutation：L236P,D238N Mutation：L236P,D238N Mutation：L236P,D238N	CA CALCIUM ION × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7；Freshly prepared gel filtration buffer, filtered through 0.22um filter and degassed cryo-EM vitrification conditions Cryogen ETHANE；Blot force -5, blot time 1 s	Resolution 3.50 Å
9NXE Crystal Structure of Calcineurin Clinical Variant E282K Deposited 2025-03-25	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–370（370 aa）	Mutation：E282K	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
9NXF Crystal structure of CN:Tak1 complex Deposited 2025-03-25	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–370（370 aa）	Mutation：D90A	FE FE (III) ION × 1 PEG DI(HYDROXYETHYL)ETHER × 2 CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.4；298 K；200 mM Sodium citrate tribasic pH 8.4, 22% PEG 3350, 3% ethanol. Microseeding	Resolution 3.13 Å R-free 0.295
9NXF Crystal structure of CN:Tak1 complex Deposited 2025-03-25	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric	Chain D 1–370（370 aa）	Mutation：D90A	FE FE (III) ION × 1 PEG DI(HYDROXYETHYL)ETHER × 1 CA CALCIUM ION × 4 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.4；298 K；200 mM Sodium citrate tribasic pH 8.4, 22% PEG 3350, 3% ethanol. Microseeding	Resolution 3.13 Å R-free 0.295
9NXN Crystal structure of CN:RII alpha Deposited 2025-03-25	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–370（370 aa）	Not recorded	CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；289 K；0.1 M sodium citrate pH 5.0, 0.1 M Magnesium chloride hexahydrate, 15% PEG 4000	Resolution 2.10 Å R-free 0.250

20 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	PP2BA_HUMAN
Isoform	Q08209-2
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–372； UniProt 1–370

Calcineurin subunit B type 1

Homo sapiens

UniProt P63098

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain B； UniProt 16–170	Not recorded	Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform × 1 （Q08209） Sodium/hydrogen exchanger 1 × 1 （P19634） 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

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 6NUF	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1AUI HUMAN CALCINEURIN HETERODIMER Deposited 1997-08-27	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–169（169 aa）	Not recorded	ZN ZINC ION × 1 FE FE (III) ION × 1 CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；PROTEIN WAS CRYSTALLIZED FROM 8% PEG 6000, 0.1M CACL2, 0.1M TES PH 7.5, 1 MM DTT.	Resolution 2.10 Å
1M63 Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes Deposited 2002-07-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain B 1–169（169 aa） Chain F 1–169（169 aa）	Not recorded	ZN ZINC ION × 2 FE FE (III) ION × 2 CA CALCIUM ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；0.1 M NA CACODYLATE, 0.2 M MGCL2, 13% PEG8000, 2.5% ETHANOL, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K	Resolution 2.80 Å R-free 0.322
1MF8 Crystal Structure of human calcineurin complexed with cyclosporin A and human cyclophilin Deposited 2002-08-09	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 0–169（170 aa）	Not recorded	PO4 PHOSPHATE ION × 1 CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；12% PEG 4000, 5MM POTASSIUM PHOSPHATE, 75MM SODIUM CITRATE, 15% GLYCEROL, 5MM TRIS, PH 4.6, MICROBATCH, TEMPERATURE 292K	Resolution 3.10 Å R-free 0.300
2P6B Crystal Structure of Human Calcineurin in Complex with PVIVIT Peptide Deposited 2007-03-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 16–170（155 aa） Fragment：Residues 16-170 Chain D 16–170（155 aa） Fragment：Residues 16-170	Not recorded	ZN ZINC ION × 2 FE FE (III) ION × 2 PO4 PHOSPHATE ION × 2 CA CALCIUM ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；295 K；12% PEG 4000, 0.1M calcium chloride, 0.1M TES, 0.001M DTT, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.30 Å R-free 0.254
3LL8 Crystal Structure of Calcineurin in Complex with AKAP79 Peptide Deposited 2010-01-28	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 16–170（155 aa） Fragment：UNP residues 16-170	Not recorded	PO4 PHOSPHATE ION × 1 ZN ZINC ION × 1 FE FE (III) ION × 1 CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；PEG 20,000 MgSO4 CaCl2, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.00 Å R-free 0.228
3LL8 Crystal Structure of Calcineurin in Complex with AKAP79 Peptide Deposited 2010-01-28	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 16–170（155 aa） Fragment：UNP residues 16-170	Not recorded	PO4 PHOSPHATE ION × 1 ZN ZINC ION × 1 FE FE (III) ION × 1 CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；PEG 20,000 MgSO4 CaCl2, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.00 Å R-free 0.228
3LL8 Crystal Structure of Calcineurin in Complex with AKAP79 Peptide Deposited 2010-01-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 16–170（155 aa） Fragment：UNP residues 16-170 Chain D 16–170（155 aa） Fragment：UNP residues 16-170	Not recorded	PO4 PHOSPHATE ION × 2 ZN ZINC ION × 2 FE FE (III) ION × 2 CA CALCIUM ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；PEG 20,000 MgSO4 CaCl2, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.00 Å R-free 0.228
4F0Z Crystal Structure of Calcineurin in Complex with the Calcineurin-Inhibiting Domain of the African Swine Fever Virus Protein A238L Deposited 2012-05-05	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–170（170 aa） Fragment：Calcineurin B Subunit	Not recorded	GOL GLYCEROL × 8 CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；295 K；0.16 M ammonium citrate dibasic, 20% (w/v) PEG3350, VAPOR DIFFUSION, SITTING DROP, temperature 295K	Resolution 1.70 Å R-free 0.178
4OR9 Crystal structure of human calcineurin Deposited 2014-02-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–170（170 aa） Fragment：regulatory subunit	Not recorded	FE FE (III) ION × 1 ZN ZINC ION × 1 CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.8；294 K；100mM MES, pH 5.8, 7% PEG3350, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.23 Å R-free 0.215
4ORA Crystal structure of a human calcineurin mutant Deposited 2014-02-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–170（170 aa）	Not recorded	ZN ZINC ION × 1 FE FE (III) ION × 1 CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.8；294 K；100 mM MES, pH 5.8, 9% PEG 3350, 4% Glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.75 Å R-free 0.249
4ORC Crystal structure of mammalian calcineurin Deposited 2014-02-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–170（170 aa） Fragment：regulatory subunit	Not recorded	ZN ZINC ION × 1 FE FE (III) ION × 1 PO4 PHOSPHATE ION × 1 CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；294 K；100mM MES, pH 6.1, 10% PEG3350, 0.2M CaCl2, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.70 Å R-free 0.260
5SVE Structure of Calcineurin in complex with NFATc1 LxVP peptide Deposited 2016-08-05	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–170（170 aa）	Not recorded	FE FE (III) ION × 1 ZN ZINC ION × 1 CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；0.1 M HEPES pH 7.0 15% Peg 4000	Resolution 2.60 Å R-free 0.239
6NUC Structure of Calcineurin in complex with NHE1 peptide Deposited 2019-01-31	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 16–170（155 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
6NUU Structure of Calcineurin mutant in complex with NHE1 peptide Deposited 2019-02-02	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 16–170（155 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
7U0T Crystal Structure of a human Calcineurin A - Calcineurin B fusion bound to FKBP12 and FK-520 Deposited 2022-02-18	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 3–170（168 aa）	Not recorded	CA CALCIUM ION × 4 EDO 1,2-ETHANEDIOL × 1 KXX (3S,4R,5S,8R,9E,12S,14S,15R,16S,18R,19R,22R,26aS)-8-ethyl-5,19-dihydroxy-3-{(1E)-1-[(1R,3R,4R)-4-hydroxy-3-methoxycyclohexyl]prop-1-en-2-yl}-14,16-dimethoxy-4,10,12,18-tetramethyl-5,6,8,11,12,13,14,15,16,17,18,19,24,25,26,26a-hexadecahydro-3H-15,19-epoxypyrido[2,1-c][1,4]oxazacyclotricosine-1,7,20,21(4H,23H)-tetrone × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；287 K；Microlytics MCSG-1 C5: 0.2M Magnesium Acetate, 20% PEG 3,350, HosaA.18272.a.TM11.PD38439 at 20mg/ml + FK-520 (Purified from SEC): cryo: 20% ethylene glycol: tray 318701c5, puck oxo8-2	Resolution 2.45 Å R-free 0.260
9B9G Structure of the PI4KA complex bound to Calcineurin Deposited 2024-04-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain H 1–170（170 aa） Chain J 1–170（170 aa）	Not recorded	CA CALCIUM ION × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7；Freshly prepared gel filtration buffer, filtered through 0.22um filter and degassed cryo-EM vitrification conditions Cryogen ETHANE；Blot force -5, blot time 1 s	Resolution 3.50 Å
9CHU Cryo-EM structure of calcineurin fused beta2 adrenergic receptor in norepinephrine bound inactive state Deposited 2024-07-02	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 16–170（155 aa）	Not recorded	E5E Noradrenaline × 1 FK5 8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.49 Å
9CHV cryo-EM structure of calcineurin-fused beta2 adrenergic receptor in apo state Deposited 2024-07-02	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 16–170（155 aa）	Not recorded	FK5 8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.95 Å
9CHX cryo-EM structure of calcineurin-fused beta2 adrenergic receptor in carazolol bound inactive state Deposited 2024-07-02	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 16–170（155 aa）	Not recorded	CAU (2S)-1-(9H-Carbazol-4-yloxy)-3-(isopropylamino)propan-2-ol × 1 FK5 8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN × 1	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	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 16–170（155 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
9NXF Crystal structure of CN:Tak1 complex Deposited 2025-03-25	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 16–170（155 aa）	Not recorded	FE FE (III) ION × 1 PEG DI(HYDROXYETHYL)ETHER × 2 CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.4；298 K；200 mM Sodium citrate tribasic pH 8.4, 22% PEG 3350, 3% ethanol. Microseeding	Resolution 3.13 Å R-free 0.295
9NXF Crystal structure of CN:Tak1 complex Deposited 2025-03-25	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric	Chain E 16–170（155 aa）	Not recorded	FE FE (III) ION × 1 PEG DI(HYDROXYETHYL)ETHER × 1 CA CALCIUM ION × 4 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.4；298 K；200 mM Sodium citrate tribasic pH 8.4, 22% PEG 3350, 3% ethanol. Microseeding	Resolution 3.13 Å R-free 0.295
9NXN Crystal structure of CN:RII alpha Deposited 2025-03-25	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–170（170 aa）	Not recorded	CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；289 K；0.1 M sodium citrate pH 5.0, 0.1 M Magnesium chloride hexahydrate, 15% PEG 4000	Resolution 2.10 Å R-free 0.250

20 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CANB1_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 2–156； UniProt 16–170

Sodium/hydrogen exchanger 1

Homo sapiens

UniProt P19634

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain C； UniProt 679–723	Mutation：R698A, R700A	Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform × 1 （Q08209） Calcineurin subunit B type 1 × 1 （P63098） 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

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 6NUF	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1Y4E NMR structure of transmembrane segment IV of the NHE1 isoform of the Na+/H+ exchanger Deposited 2004-11-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	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	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	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
6NUU Structure of Calcineurin mutant in complex with NHE1 peptide Deposited 2019-02-02	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	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	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	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	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	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

18 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	SL9A1_HUMAN
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain C； PDBConstruct 4–48； UniProt 679–723

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	6nuf
Deposition date deposition_date	2019-01-31
Structure title title	Structure of Calcineurin in complex with NHE1 peptide
Keywords keywords	Ser/thr phosphatase, complex, HYDROLASE, HYDROLASE-Calcium Binding Protein complex; HYDROLASE/Calcium Binding Protein
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	29.76 Å
Radius of gyration Rg (electron density) rg_electron	29.36 Å
Forward intensity I(0) i0	60295600.00
Molecular weight molecular_weight	61871.0 kDa
Excluded volume excluded_volume	77625 Å³
Envelope volume envelope_volume	93023 Å³
Hydration-shell volume shell_volume	28029 Å³
Envelope diameter envelope_diameter	104.5 Å
Shell Rg shell_rg	34.34 Å
Envelope Rg envelope_rg	29.72 Å
Shape Rg shape_rg	29.34 Å
Total Rg total_rg	29.89 Å
Total atoms total_atoms	8583
Residues n_residues	535
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	102.0 Å
Rg (real space) rg_real	30.04 Å
Rg uncertainty (real space) rg_real_error	1.15 Å
I(0) (real space) i0_real	6.0300e+07
I(0) uncertainty (real space) i0_real_error	1.0280e+06
Rg (reciprocal space) rg_reciprocal	29.92 Å
I(0) (reciprocal space) i0_reciprocal	60290000.0000
Solution quality estimate total_estimate	0.8106
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	26.9 Å
Skewness Skewness skewness	0.544
Kurtosis Kurtosis kurtosis	-0.407
Angular range angular_range	— – 0.2650 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	17420000.0000
Real-space data points n_real_points	54
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.639; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.721; Smooth: 0.901

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (11)

Entity 1 Entity 1 polymer

Description description	Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform
Molecular weight formula_weight	42855.0 kDa
EC 编号 ec_number	3.1.3.16
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	9109

GHMSEPKAIDPKLSTTDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKEGRLEESVALRIITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEINTLDDIRKLDRFKEPPAYGPMCDILWSDPLEDFGNEKTQEHFTHNTVRGCSYFYSYPAVCEFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLN

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	Human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Calcineurin subunit B type 1
Molecular weight formula_weight	17755.2 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

MDADEIKRLGKRFKKLDLDNSGSLSVEEFMSLPELQQNPLVQRVIDIFDTDGNGEVDFKEFIEGVSQFSVKGDKEQKLRFAFRIYDMDKDGYISNGELFQVLKMMVGNNLKDTQLQQIVDKTIINADKDGDGRISFEEFCAVVGGLDIHKKMVVDV

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	Human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 3 Entity 3 polymer

Description description	Sodium/hydrogen exchanger 1
Molecular weight formula_weight	5095.8 kDa
Mutation mutation	R698A, R700A
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

GHMKINNYLTVPAHKLDSPTMSAAAIGSDPLAYEPKEDLPVITIDPAS

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	Human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 4 Entity 4 non-polymer

Description description	FE (III) ION
Molecular weight formula_weight	55.8 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 6 Entity 6 non-polymer

Description description	PHOSPHATE ION
Molecular weight formula_weight	95.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 7 Entity 7 non-polymer

Description description	TRIETHYLENE GLYCOL
Molecular weight formula_weight	150.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 8 Entity 8 non-polymer

Description description	DI(HYDROXYETHYL)ETHER
Molecular weight formula_weight	106.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 9 Entity 9 non-polymer

Description description	SODIUM ION
Molecular weight formula_weight	23.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 10 Entity 10 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 11 Entity 11 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	471

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7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d6nufa_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.159 — Metallo-dependent phosphatases
Superfamily Superfamily superfamily	d.159.1 — Metallo-dependent phosphatases
Family Family family	d.159.1.3 — Protein serine/threonine phosphatase

Domain ID domain_id	d6nufb1
Class class	a — All alpha proteins
Fold Fold fold	a.39 — EF Hand-like
Superfamily Superfamily superfamily	a.39.1 — EF-hand
Family Family family	a.39.1.5 — Calmodulin-like

Domain ID domain_id	d6nufb2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id	6nufA00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	21 — Purple Acid Phosphatase; chain A, domain 2
Homologous superfamily homologous superfamily	10 — Metallo-dependent phosphatases

Domain ID domain_id	6nufB00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

▶

8. Citations (1)

▶

Unit-cell length a length_a	79.477 Å
Unit-cell length b length_b	126.808 Å
Unit-cell length c length_c	127.431 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	—

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	16.130 Å
R factor r_factor	0.1710
R_work r_work	0.1690
R_free r_free	0.2090

fit	/app/data/saxs_computation/nu/6nuf/6nuf.fit
pddf	/app/data/pr_computation/nu/6nuf/6nuf.pr.out
profile	/app/data/saxs_computation/nu/6nuf/6nuf.dat

Structure of Calcineurin in complex with NHE1 peptide

1. Protein Identity and Related Structures Protein Identity & Related Structures

Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform

State in the Current Structure

Other States of the Same Protein in the Database

Calcineurin subunit B type 1

State in the Current Structure

Other States of the Same Protein in the Database

Sodium/hydrogen exchanger 1

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (11)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 non-polymer

Entity 8 Entity 8 non-polymer

Entity 9 Entity 9 non-polymer

Entity 10 Entity 10 non-polymer

Entity 11 Entity 11 water

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)