SAXSdb — 9b9g

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

Phosphatidylinositol 4-kinase alpha

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 × 10 PDB declaration: decameric（10） Consistent with protein copy count	Chain A； UniProt 1–2102 Chain B； UniProt 1–2102	Not recorded	Tetratricopeptide repeat protein 7B × 2 （Q86TV6） Hyccin × 2 （Q9BYI3） Calcineurin subunit B type 1 × 2 （P63098） Protein phosphatase 3 catalytic subunit alpha × 2 （Q08209） 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

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 9B9G	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6BQ1 Human PI4KIIIa lipid kinase complex Deposited 2017-11-27	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 932–2102（1171 aa） Chain E 932–2102（1171 aa）	Not recorded	E4S 5-{2-amino-1-[4-(morpholin-4-yl)phenyl]-1H-benzimidazol-6-yl}-N-(2-fluorophenyl)-2-methoxypyridine-3-sulfonamide × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
9BAX PI4KA complex bound to C-terminus of EFR3A Deposited 2024-04-04	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 1–2102（2102 aa） Chain B 1–2102（2102 aa）	Not recorded	No recorded non-water small molecule	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 1.5 s	Resolution 3.65 Å
9OT6 Cryo-EM structure of the PI4KA complex bound to an EFR3 interfering nanobody (F3IN) Deposited 2025-05-26	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 1–2102（2102 aa） Chain B 1–2102（2102 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE；Blot force -5, blot time 1.5 s.	Resolution 3.54 Å

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	PI4KA_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–2102； UniProt 1–2102 Author chain B； PDBConstruct 1–2102； UniProt 1–2102

Tetratricopeptide repeat protein 7B

Homo sapiens

UniProt Q86TV6

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 × 10 PDB declaration: decameric（10） Consistent with protein copy count	Chain D； UniProt 1–843 Chain F； UniProt 1–843	Not recorded	Phosphatidylinositol 4-kinase alpha × 2 （P42356） Hyccin × 2 （Q9BYI3） Calcineurin subunit B type 1 × 2 （P63098） Protein phosphatase 3 catalytic subunit alpha × 2 （Q08209） 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

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 9B9G	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
5DSE Crystal Structure of the TTC7B/Hyccin Complex Deposited 2015-09-17	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 A 7–843（837 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；1.35 ul protein + 1.35 ul mother liquor (0.1 M HEPES [pH 7.0-7.4], 4-5% polyethylene glycol [PEG] 8,000) + 0.3 ul 0.2 M 3-(1-Pyridino)-1-propane sulfonate (NDSB-201)	Resolution 2.90 Å R-free 0.242
5DSE Crystal Structure of the TTC7B/Hyccin Complex Deposited 2015-09-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 7–843（837 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；1.35 ul protein + 1.35 ul mother liquor (0.1 M HEPES [pH 7.0-7.4], 4-5% polyethylene glycol [PEG] 8,000) + 0.3 ul 0.2 M 3-(1-Pyridino)-1-propane sulfonate (NDSB-201)	Resolution 2.90 Å R-free 0.242
6BQ1 Human PI4KIIIa lipid kinase complex Deposited 2017-11-27	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 1–843（843 aa） Chain F 1–843（843 aa）	Not recorded	E4S 5-{2-amino-1-[4-(morpholin-4-yl)phenyl]-1H-benzimidazol-6-yl}-N-(2-fluorophenyl)-2-methoxypyridine-3-sulfonamide × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
9BAX PI4KA complex bound to C-terminus of EFR3A Deposited 2024-04-04	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain D 1–843（843 aa） Chain F 1–843（843 aa）	Not recorded	No recorded non-water small molecule	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 1.5 s	Resolution 3.65 Å
9OT6 Cryo-EM structure of the PI4KA complex bound to an EFR3 interfering nanobody (F3IN) Deposited 2025-05-26	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain D 1–843（843 aa） Chain F 1–843（843 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE；Blot force -5, blot time 1.5 s.	Resolution 3.54 Å

4 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TTC7B_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain D； PDBConstruct 1–843； UniProt 1–843 Author chain F； PDBConstruct 1–843； UniProt 1–843

Hyccin

Homo sapiens

UniProt Q9BYI3

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 × 10 PDB declaration: decameric（10） Consistent with protein copy count	Chain E； UniProt 1–308 Chain G； UniProt 1–308	Not recorded	Phosphatidylinositol 4-kinase alpha × 2 （P42356） Tetratricopeptide repeat protein 7B × 2 （Q86TV6） Calcineurin subunit B type 1 × 2 （P63098） Protein phosphatase 3 catalytic subunit alpha × 2 （Q08209） 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

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 9B9G	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
5DSE Crystal Structure of the TTC7B/Hyccin Complex Deposited 2015-09-17	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 2–308（307 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；1.35 ul protein + 1.35 ul mother liquor (0.1 M HEPES [pH 7.0-7.4], 4-5% polyethylene glycol [PEG] 8,000) + 0.3 ul 0.2 M 3-(1-Pyridino)-1-propane sulfonate (NDSB-201)	Resolution 2.90 Å R-free 0.242
5DSE Crystal Structure of the TTC7B/Hyccin Complex Deposited 2015-09-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 2–308（307 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；1.35 ul protein + 1.35 ul mother liquor (0.1 M HEPES [pH 7.0-7.4], 4-5% polyethylene glycol [PEG] 8,000) + 0.3 ul 0.2 M 3-(1-Pyridino)-1-propane sulfonate (NDSB-201)	Resolution 2.90 Å R-free 0.242
6BQ1 Human PI4KIIIa lipid kinase complex Deposited 2017-11-27	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain C 2–289（288 aa） Chain G 2–289（288 aa）	Not recorded	E4S 5-{2-amino-1-[4-(morpholin-4-yl)phenyl]-1H-benzimidazol-6-yl}-N-(2-fluorophenyl)-2-methoxypyridine-3-sulfonamide × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
9BAX PI4KA complex bound to C-terminus of EFR3A Deposited 2024-04-04	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 1–308（308 aa） Chain G 1–308（308 aa）	Not recorded	No recorded non-water small molecule	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 1.5 s	Resolution 3.65 Å
9OT6 Cryo-EM structure of the PI4KA complex bound to an EFR3 interfering nanobody (F3IN) Deposited 2025-05-26	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 1–308（308 aa） Fragment：residues 1-308 Chain G 1–308（308 aa） Fragment：residues 1-308	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE；Blot force -5, blot time 1.5 s.	Resolution 3.54 Å

4 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	HYCCI_HUMAN
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain E； PDBConstruct 1–308； UniProt 1–308 Author chain G； PDBConstruct 1–308； UniProt 1–308

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 × 10 PDB declaration: decameric（10） Consistent with protein copy count	Chain H； UniProt 1–170 Chain J； UniProt 1–170	Not recorded	Phosphatidylinositol 4-kinase alpha × 2 （P42356） Tetratricopeptide repeat protein 7B × 2 （Q86TV6） Hyccin × 2 （Q9BYI3） Protein phosphatase 3 catalytic subunit alpha × 2 （Q08209） 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

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 9B9G	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 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 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 oligomeric state Different ligand/ion Different experimental method 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 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 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 oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state 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 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 method 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 oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state 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 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 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 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 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 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 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 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 mutation/modification Different oligomeric state 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 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 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 × 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
6NUF Structure of Calcineurin in complex with NHE1 peptide Deposited 2019-01-31	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 × 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 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	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 × 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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
9CHU Cryo-EM structure of calcineurin fused beta2 adrenergic receptor in norepinephrine bound inactive state Deposited 2024-07-02	Different construct 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 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 construct 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 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 construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions	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 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 × 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 construct Different mutation/modification 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 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 construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state 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 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	4
Chains and sequence ranges	Author chain H； PDBConstruct 1–170； UniProt 1–170 Author chain J； PDBConstruct 1–170； UniProt 1–170

Protein phosphatase 3 catalytic subunit alpha

Homo sapiens

UniProt Q08209

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 × 10 PDB declaration: decameric（10） Consistent with protein copy count	Chain I； UniProt 2–391 Chain I； UniProt 162–391 Chain K； UniProt 2–391 Chain K； UniProt 162–391	Mutation：L236P,D238N	Phosphatidylinositol 4-kinase alpha × 2 （P42356） Tetratricopeptide repeat protein 7B × 2 （Q86TV6） Hyccin × 2 （Q9BYI3） Calcineurin subunit B type 1 × 2 （P63098） 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

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 9B9G	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 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 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 method 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 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 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 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 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 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 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 method 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 experimental method 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 method 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 method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 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 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 method 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 method 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 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 × 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 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 × 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
6NUF Structure of Calcineurin in complex with NHE1 peptide Deposited 2019-01-31	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 × 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 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	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 × 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 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 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
9NXE Crystal Structure of Calcineurin Clinical Variant E282K Deposited 2025-03-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein 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 construct Different mutation/modification 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 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 construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 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 × 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	—
PDB entities	5
Chains and sequence ranges	Author chain I； PDBConstruct 1–390； UniProt 2–391 Author chain I； PDBConstruct 391–620； UniProt 162–391 Author chain K； PDBConstruct 1–390； UniProt 2–391 Author chain K； PDBConstruct 391–620； UniProt 162–391

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	9b9g
Deposition date deposition_date	2024-04-02
Structure title title	Structure of the PI4KA complex bound to Calcineurin
Keywords keywords	PI4KIIIa complex, PI4KA, TTC7B, FAM126A, CNA, CNB, Calcineurin, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	78.99 Å
Radius of gyration Rg (electron density) rg_electron	79.06 Å
Forward intensity I(0) i0	6160680000.00
Molecular weight molecular_weight	692110.0 kDa
Excluded volume excluded_volume	876440 Å³
Envelope volume envelope_volume	1609800 Å³
Hydration-shell volume shell_volume	170750 Å³
Envelope diameter envelope_diameter	279.4 Å
Shell Rg shell_rg	76.78 Å
Envelope Rg envelope_rg	75.38 Å
Shape Rg shape_rg	79.06 Å
Total Rg total_rg	79.03 Å
Total atoms total_atoms	48664
Residues n_residues	6075
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	282.1 Å
Rg (real space) rg_real	83.23 Å
Rg uncertainty (real space) rg_real_error	1.96 Å
I(0) (real space) i0_real	6.1960e+09
I(0) uncertainty (real space) i0_real_error	1.4240e+08
Rg (reciprocal space) rg_reciprocal	78.88 Å
I(0) (reciprocal space) i0_reciprocal	6158000000.0000
Solution quality estimate total_estimate	0.9026
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	84.6 Å
Skewness Skewness skewness	0.489
Kurtosis Kurtosis kurtosis	-0.065
Angular range angular_range	— – 0.1000 Å⁻¹
Current regularization parameter α current_alpha	1.1020
Highest regularization parameter α highest_alpha	449800000.0000
Real-space data points n_real_points	21
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.866; Stabil: 0.857; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.608

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	Phosphatidylinositol 4-kinase alpha
Molecular weight formula_weight	237102.3 kDa
EC 编号 ec_number	2.7.1.67
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	48676

MAAAPARGGGGGGGGGGGCSGSGSSASRGFYFNTVLSLARSLAVQRPASLEKVQKLLCMCPVDFHGIFQLDERRRDAVIALGIFLIESDLQHKDCVVPYLLRLLKGLPKVYWVEESTARKGRGALPVAESFSFCLVTLLSDVAYRDPSLRDEILEVLLQVLHVLLGMCQALEIQDKEYLCKYAIPCLIGISRAFGRYSNMEESLLSKLFPKIPPHSLRVLEELEGVRRRSFNDFRSILPSNLLTVCQEGTLKRKTSSVSSISQVSPERGMPPPSSPGGSAFHYFEASCLPDGTALEPEYYFSTISSSFSVSPLFNGVTYKEFNIPLEMLRELLNLVKKIVEEAVLKSLDAIVASVMEANPSADLYYTSFSDPLYLTMFKMLRDTLYYMKDLPTSFVKEIHDFVLEQFNTSQGELQKILHDADRIHNELSPLKLRCQANAACVDLMVWAVKDEQGAENLCIKLSEKLQSKTSSKVIIAHLPLLICCLQGLGRLCERFPVVVHSVTPSLRDFLVIPSPVLVKLYKYHSQYHTVAGNDIKISVTNEHSESTLNVMSGKKSQPSMYEQLRDIAIDNICRCLKAGLTVDPVIVEAFLASLSNRLYISQESDKDAHLIPDHTIRALGHIAVALRDTPKVMEPILQILQQKFCQPPSPLDVLIIDQLGCLVITGNQYIYQEVWNLFQQISVKASSVVYSATKDYKDHGYRHCSLAVINALANIAANIQDEHLVDELLMNLLELFVQLGLEGKRASERASEKGPALKASSSAGNLGVLIPVIAVLTRRLPPIKEAKPRLQKLFRDFWLYSVLMGFAVEGSGLWPEEWYEGVCEIATKSPLLTFPSKEPLRSVLQYNSAMKNDTVTPAELSELRSTIINLLDPPPEVSALINKLDFAMSTYLLSVYRLEYMRVLRSTDPDRFQVMFCYFEDKAIQKDKSGMMQCVIAVADKVFDAFLNMMADKAKTKENEEELERHAQFLLVNFNHIHKRIRRVADKYLSGLVDKFPHLLWSGTVLKTMLDILQTLSLSLSADIHKDQPYYDIPDAPYRITVPDTYEARESIVKDFAARCGMILQEAMKWAPTVTKSHLQEYLNKHQNWVSGLSQHTGLAMATESILHFAGYNKQNTTLGATQLSERPACVKKDYSNFMASLNLRNRYAGEVYGMIRFSGTTGQMSDLNKMMVQDLHSALDRSHPQHYTQAMFKLTAMLISSKDCDPQLLHHLCWGPLRMFNEHGMETALACWEWLLAGKDGVEVPFMREMAGAWHMTVEQKFGLFSAEIKEADPLAASEASQPKPCPPEVTPHYIWIDFLVQRFEIAKYCSSDQVEIFSSLLQRSMSLNIGGAKGSMNRHVAAIGPRFKLLTLGLSLLHADVVPNATIRNVLREKIYSTAFDYFSCPPKFPTQGEKRLREDISIMIKFWTAMFSDKKYLTASQLVPPDNQDTRSNLDITVGSRQQATQGWINTYPLSSGMSTISKKSGMSKKTNRGSQLHKYYMKRRTLLLSLLATEIERLITWYNPLSAPELELDQAGENSVANWRSKYISLSEKQWKDNVNLAWSISPYLAVQLPARFKNTEAIGNEVTRLVRLDPGAVSDVPEAIKFLVTWHTIDADAPELSHVLCWAPTDPPTGLSYFSSMYPPHPLTAQYGVKVLRSFPPDAILFYIPQIVQALRYDKMGYVREYILWAASKSQLLAHQFIWNMKTNIYLDEEGHQKDPDIGDLLDQLVEEITGSLSGPAKDFYQREFDFFNKITNVSAIIKPYPKGDERKKACLSALSEVKVQPGCYLPSNPEAIVLDIDYKSGTPMQSAAKAPYLAKFKVKRCGVSELEKEGLRCRSDSEDECSTQEADGQKISWQAAIFKVGDDCRQDMLALQIIDLFKNIFQLVGLDLFVFPYRVVATAPGCGVIECIPDCTSRDQLGRQTDFGMYDYFTRQYGDESTLAFQQARYNFIRSMAAYSLLLFLLQIKDRHNGNIMLDKKGHIIHIDFGFMFESSPGGNLGWEPDIKLTDEMVMIMGGKMEATPFKWFMEMCVRGYLAVRPYMDAVVSLVTLMLDTGLPCFRGQTIKLLKHRFSPNMTEREAANFIMKVIQSCFLSNRSRTYDMIQYYQNDIPY

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	Spodoptera frugiperda

Entity 2 Entity 2 polymer

Description description	Tetratricopeptide repeat protein 7B
Molecular weight formula_weight	94294.1 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,F

MATKKAGSRLETEIERCRSECQWERIPELVKQLSAKLIANDDMAELLLGESKLEQYLKEHPLRQGASPRGPKPQLTEVRKHLTAALDRGNLKSEFLQESNLIMAKLNYVEGDYKEALNIYARVGLDDLPLTAVPPYRLRVIAEAYATKGLCLEKLPISSSTSNLHVDREQDVITCYEKAGDIALLYLQEIERVILSNIQNRSPKPGPAPHDQELGFFLETGLQRAHVLYFKNGNLTRGVGRFRELLRAVETRTTQNLRMTIARQLAEILLRGMCEQSYWNPLEDPPCQSPLDDPLRKGANTKTYTLTRRARVYSGENIFCPQENTEEALLLLLISESMANRDAVLSRIPEHKSDRLISLQSASVVYDLLTIALGRRGQYEMLSECLERAMKFAFEEFHLWYQFALSLMAAGKSARAVKVLKECIRLKPDDATIPLLAAKLCMGSLHWLEEAEKFAKTVVDVGEKTSEFKAKGYLALGLTYSLQATDASLRGMQEVLQRKALLAFQRAHSLSPTDHQAAFYLALQLAISRQIPEALGYVRQALQLQGDDANSLHLLALLLSAQKHYHDALNIIDMALSEYPENFILLFSKVKLQSLCRGPDEALLTCKHMLQIWKSCYNLTNPSDSGRGSSLLDRTIADRRQLNTITLPDFSDPETGSVHATSVAASRVEQALSEVASSLQSSAPKQGPLHPWMTLAQIWLHAAEVYIGIGKPAEATACTQEAANLFPMSHNVLYMRGQIAELRGSMDEARRWYEEALAISPTHVKSMQRLALILHQLGRYSLAEKILRDAVQVNSTAHEVWNGLGEVLQAQGNDAAATECFLTALELEASSPAVPFTIIPRVL

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	Spodoptera frugiperda

Entity 3 Entity 3 polymer

Description description	Hyccin
Molecular weight formula_weight	34638.9 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,G

MFTSEKGVVEEWLSEFKTLPETSLPNYATNLKDKSSLVSSLYKVIQEPQSELLEPVCHQLFEFYRSGEEQLLQFTLQFLPELIWCYLAVSASRNVHSSGCIEALLLGVYNLEIVDKQGHTKVLSFTIPSLSKPSVYHEPSSIGSMALTESALSQHGLSKVVYSGPHPQREMLTAQNRFEVLTFLLLCYNAALTYMPSVSLQSLCQICSRICVCGYPRQHVRKYKGISSRIPVSSGFMVQMLTGIYFAFYNGEWDLAQKALDDIIYRAQLELYPEPLLVANAIKASLPHGPMKSNKEGTRCIQVEITPT

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	Spodoptera frugiperda

Entity 4 Entity 4 polymer

Description description	Calcineurin subunit B type 1
Molecular weight formula_weight	19322.9 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H,J

MGNEASYPLEMCSHFDADEIKRLGKRFKKLDLDNSGSLSVEEFMSLPELQQNPLVQRVIDIFDTDGNGEVDFKEFIEGVSQFSVKGDKEQKLRFAFRIYDMDKDGYISNGELFQVLKMMVGNNLKDTQLQQIVDKTIINADKDGDGRISFEEFCAVVGGLDIHKKMVVDV

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 BL21(DE3)

Entity 5 Entity 5 polymer

Description description	Protein phosphatase 3 catalytic subunit alpha
Molecular weight formula_weight	70883.2 kDa
EC 编号 ec_number	3.1.3.16
Mutation mutation	L236P,D238N
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	I,K

SEPKAIDPKLSTTDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKEGRLEESVALRIITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEINTLDDIRKLDRFKEPPAYGPMCDILWSDPPENFGNEKTQEHFTHNTVRGCSYFYSYPAVCEFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLNICSDDELGSEEDGFDGATAAAFKQECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEINTLDDIRKLDRFKEPPAYGPMCDILWSDPPEDFGNEKTQEHFTHNTVRGCSYFYSYPAVCEFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLNICSDDELGSEEDGFDGATAAA

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 BL21(DE3)

Entity 6 Entity 6 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	8

▶

8. Citations (1)

▶

Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	—

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	3.50 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	235760

fit	/app/data/saxs_computation/b9/9b9g/9b9g.fit
pddf	/app/data/pr_computation/b9/9b9g/9b9g.pr.out
profile	/app/data/saxs_computation/b9/9b9g/9b9g.dat

Structure of the PI4KA complex bound to Calcineurin

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

Phosphatidylinositol 4-kinase alpha

State in the Current Structure

Other States of the Same Protein in the Database

Tetratricopeptide repeat protein 7B

State in the Current Structure

Other States of the Same Protein in the Database

Hyccin

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

Protein phosphatase 3 catalytic subunit alpha

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (6)

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 polymer

Polymer Polymer

来源 Source

Entity 5 Entity 5 polymer

Polymer Polymer

来源 Source

Entity 6 Entity 6 non-polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)