7aam

Crystal structure of the F-BAR domain of PSTIPIP1 bound to the CTH domain of the phosphatase LYP

Method: X-RAY DIFFRACTION D_max: 226.1 Å Quality: REASONABLE

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

Proline-serine-threonine phosphatase-interacting protein 1

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 1–289 Chain B； UniProt 1–289	Not recorded	Tyrosine-protein phosphatase non-receptor type 22 × 1 （Q9Y2R2） GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；100 mM Bis-Tris-propane (pH=6.0), 20% (w/v) PEG 3350, 200 mM sodium citrate. LYP-CTH peptide was soaked into preformed crystals of the F-BAR domain of PSTPIP1.	Resolution 2.15 Å R-free 0.241

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 7AAM	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2DIL Solution structure of the SH3 domain of the human Proline-serine-threonine phosphatase-interacting protein 1 Deposited 2006-03-30	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 361–416（56 aa） Fragment：SH3 domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 120；Pressure ambient NMR sample composition 1.07mM SH3 domian U-15N,13C; 20mM d-Tris HCl (pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O, 10% D2O' \| 90% H2O/10% D2O	Resolution not provided
7AAL Crystal structure of the F-BAR domain of PSTIPIP1, G258A mutant Deposited 2020-09-04	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–289（289 aa） Chain B 1–289（289 aa）	Mutation：G258A Mutation：G258A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；100 mM Bis-Tris-propane (pH 6.5), 15% (w/v) PEG 3350, 0.25 M sodium citrate	Resolution 1.97 Å R-free 0.219
7AAN Crystal structure of the F-BAR domain of PSTIPIP1 Deposited 2020-09-04	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–289（289 aa） Chain B 1–289（289 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；100 mM Bis-Tris-propane (pH=6.0), 17% (w/v) PEG 3350, 150 mM sodium citrate	Resolution 2.14 Å R-free 0.240

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

View Construct and Data Evidence

UniProt name	PPIP1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–292； UniProt 1–289 Author chain B； PDBConstruct 4–292； UniProt 1–289

Tyrosine-protein phosphatase non-receptor type 22

OrganismNot specified

UniProt Q9Y2R2

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 787–807	Not recorded	Proline-serine-threonine phosphatase-interacting protein 1 × 2 （O43586） GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；100 mM Bis-Tris-propane (pH=6.0), 20% (w/v) PEG 3350, 200 mM sodium citrate. LYP-CTH peptide was soaked into preformed crystals of the F-BAR domain of PSTPIP1.	Resolution 2.15 Å R-free 0.241

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 7AAM	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2P6X Crystal structure of human tyrosine phosphatase PTPN22 Deposited 2007-03-19	Different construct 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 1–302（302 aa） Fragment：PTPN22, Tyrosine-protein phosphatase catalytic domain	Not recorded	EDO 1,2-ETHANEDIOL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.9；293 K；100 mM Bicine pH 7.9, 25% PEG 10000, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 1.90 Å R-free 0.217
2P6X Crystal structure of human tyrosine phosphatase PTPN22 Deposited 2007-03-19	Different construct 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 1–302（302 aa） Fragment：PTPN22, Tyrosine-protein phosphatase catalytic domain	Not recorded	EDO 1,2-ETHANEDIOL × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.9；293 K；100 mM Bicine pH 7.9, 25% PEG 10000, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 1.90 Å R-free 0.217
2QCJ Native Structure of Lyp Deposited 2007-06-19	Different construct 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 1–294（294 aa） Fragment：catalytic domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 5.6；293 K；20% PEG 3350, pH 5.6, EVAPORATION, temperature 293K	Resolution 3.00 Å R-free 0.307
2QCJ Native Structure of Lyp Deposited 2007-06-19	Different construct 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 1–294（294 aa） Fragment：catalytic domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 5.6；293 K；20% PEG 3350, pH 5.6, EVAPORATION, temperature 293K	Resolution 3.00 Å R-free 0.307
2QCT Structure of Lyp with inhibitor I-C11 Deposited 2007-06-19	Different construct 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 1–294（294 aa） Fragment：catalytic domain	Not recorded	561 6-HYDROXY-3-{(4R)-1-[4-(1-NAPHTHYLAMINO)-4-OXOBUTYL]-1,2,3-TRIAZOLIDIN-4-YL}-1-BENZOFURAN-5-CARBOXYLIC ACID × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 7.2；293 K；0.2M sodium formate, 20% PEG3350, 2.5% ethyl glycerol, pH 7.2, EVAPORATION, temperature 293K	Resolution 2.80 Å R-free 0.275
2QCT Structure of Lyp with inhibitor I-C11 Deposited 2007-06-19	Different construct 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 1–294（294 aa） Fragment：catalytic domain	Not recorded	EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 7.2；293 K；0.2M sodium formate, 20% PEG3350, 2.5% ethyl glycerol, pH 7.2, EVAPORATION, temperature 293K	Resolution 2.80 Å R-free 0.275
3BRH Protein Tyrosine Phosphatase PTPN-22 (Lyp) bound to the mono-Phosphorylated Lck active site peptide Deposited 2007-12-21	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 1–310（310 aa） Fragment：Substrate Trapped Catalytic Domain	Mutation：D195A, C227S	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100mM Bicine, 20% PEG6000, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.20 Å R-free 0.264
3BRH Protein Tyrosine Phosphatase PTPN-22 (Lyp) bound to the mono-Phosphorylated Lck active site peptide Deposited 2007-12-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–310（310 aa） Fragment：Substrate Trapped Catalytic Domain	Mutation：D195A, C227S	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100mM Bicine, 20% PEG6000, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.20 Å R-free 0.264
3H2X Crystal Structure of The Human Lymphoid Tyrosine Phosphatase Catalytic Domain Deposited 2009-04-14	Different construct 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 1–302（302 aa） Fragment：Catalytic Domain	Not recorded	PO4 PHOSPHATE ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.2；291.15 K；2.0 M (NH4)2SO4, 0.1 M MES, 0.2 M Na/KPO4, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 291.15K	Resolution 2.20 Å R-free 0.204
3OLR PTPN22 in complex with consensus phospho-tyrosine peptide 1 Deposited 2010-08-26	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 1–294（294 aa） Fragment：UNP residues 1-294	Mutation：C227S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；20% PEG 3350, 0.1M Tris-Hcl, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.210
3OLR PTPN22 in complex with consensus phospho-tyrosine peptide 1 Deposited 2010-08-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–294（294 aa） Fragment：UNP residues 1-294	Mutation：C227S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；20% PEG 3350, 0.1M Tris-Hcl, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.210
3OLR PTPN22 in complex with consensus phospho-tyrosine peptide 1 Deposited 2010-08-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–294（294 aa） Fragment：UNP residues 1-294	Mutation：C227S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；20% PEG 3350, 0.1M Tris-Hcl, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.210
3OLR PTPN22 in complex with consensus phospho-tyrosine peptide 1 Deposited 2010-08-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–294（294 aa） Fragment：UNP residues 1-294	Mutation：C227S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；20% PEG 3350, 0.1M Tris-Hcl, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.210
3OMH Crystal structure of PTPN22 in complex with SKAP-HOM pTyr75 peptide Deposited 2010-08-26	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 1–294（294 aa） Fragment：Tyrosine-protein phosphatase domain residues 1-294	Mutation：C227S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；293 K；20% PEG 3350, 0.1M Tris-Hcl, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.90 Å R-free 0.260
3OMH Crystal structure of PTPN22 in complex with SKAP-HOM pTyr75 peptide Deposited 2010-08-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–294（294 aa） Fragment：Tyrosine-protein phosphatase domain residues 1-294	Mutation：C227S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；293 K；20% PEG 3350, 0.1M Tris-Hcl, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.90 Å R-free 0.260
3OMH Crystal structure of PTPN22 in complex with SKAP-HOM pTyr75 peptide Deposited 2010-08-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–294（294 aa） Fragment：Tyrosine-protein phosphatase domain residues 1-294	Mutation：C227S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；293 K；20% PEG 3350, 0.1M Tris-Hcl, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.90 Å R-free 0.260
3OMH Crystal structure of PTPN22 in complex with SKAP-HOM pTyr75 peptide Deposited 2010-08-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–294（294 aa） Fragment：Tyrosine-protein phosphatase domain residues 1-294	Mutation：C227S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；293 K；20% PEG 3350, 0.1M Tris-Hcl, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.90 Å R-free 0.260
4J51 Cyrstal structure of protein tyrosine phosphatase Lyp catalytic domain complex with small molecular inhibitor L75N04 Deposited 2013-02-07	Different construct 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 1–303（303 aa）	Not recorded	N75 3-[(3-chlorophenyl)ethynyl]-2-{4-[2-(cyclopropylamino)-2-oxoethoxy]phenyl}-6-hydroxy-1-benzofuran-5-carboxylic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.2；298 K；0.2 M sodium formate (pH 7.2) and 20% PEG3350, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.30 Å R-free 0.238
4J51 Cyrstal structure of protein tyrosine phosphatase Lyp catalytic domain complex with small molecular inhibitor L75N04 Deposited 2013-02-07	Different construct 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 1–303（303 aa）	Not recorded	N75 3-[(3-chlorophenyl)ethynyl]-2-{4-[2-(cyclopropylamino)-2-oxoethoxy]phenyl}-6-hydroxy-1-benzofuran-5-carboxylic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.2；298 K；0.2 M sodium formate (pH 7.2) and 20% PEG3350, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.30 Å R-free 0.238
9YDM Targeting PTPN22 at non-orthosteric binding sites - a fragment approach Deposited 2025-09-22	Different construct 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 1–303（303 aa）	Not recorded	EOH ETHANOL × 1 GOL GLYCEROL × 3 SO4 SULFATE ION × 1 A1CU3 N-(3-methyl-1H-pyrazol-5-yl)-3-phenylpropanamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；292.15 K；0.1 M HEPES pH 7.5, 0.2 M MgCl2, and 25% PEG 3350	Resolution 1.99 Å R-free 0.276
9YDM Targeting PTPN22 at non-orthosteric binding sites - a fragment approach Deposited 2025-09-22	Different construct 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 1–303（303 aa）	Not recorded	EOH ETHANOL × 1 GOL GLYCEROL × 2 A1CU3 N-(3-methyl-1H-pyrazol-5-yl)-3-phenylpropanamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；292.15 K；0.1 M HEPES pH 7.5, 0.2 M MgCl2, and 25% PEG 3350	Resolution 1.99 Å R-free 0.276
9YG0 Targeting PTPN22 at non-orthosteric binding sites - a fragment approach Deposited 2025-09-27	Different construct 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 1–303（303 aa）	Not recorded	GOL GLYCEROL × 1 EOH ETHANOL × 1 MG MAGNESIUM ION × 1 A1CWM 1-[(3S)-3-amino-2,3-dihydro-1H-indol-1-yl]-3-phenylpropan-1-one × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；292.15 K；PEGII C9: 0.1 M TRIS pH 8.5, 0.2 M magnesium chloride, & 16 % PEG 4000	Resolution 1.76 Å R-free 0.240
9YG0 Targeting PTPN22 at non-orthosteric binding sites - a fragment approach Deposited 2025-09-27	Different construct 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 1–303（303 aa）	Not recorded	EOH ETHANOL × 2 MG MAGNESIUM ION × 3 A1CWM 1-[(3S)-3-amino-2,3-dihydro-1H-indol-1-yl]-3-phenylpropan-1-one × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；292.15 K；PEGII C9: 0.1 M TRIS pH 8.5, 0.2 M magnesium chloride, & 16 % PEG 4000	Resolution 1.76 Å R-free 0.240
9YG0 Targeting PTPN22 at non-orthosteric binding sites - a fragment approach Deposited 2025-09-27	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 1–303（303 aa）	Not recorded	EOH ETHANOL × 1 MG MAGNESIUM ION × 1 A1CWM 1-[(3S)-3-amino-2,3-dihydro-1H-indol-1-yl]-3-phenylpropan-1-one × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；292.15 K；PEGII C9: 0.1 M TRIS pH 8.5, 0.2 M magnesium chloride, & 16 % PEG 4000	Resolution 1.76 Å R-free 0.240
9YG0 Targeting PTPN22 at non-orthosteric binding sites - a fragment approach Deposited 2025-09-27	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 1–303（303 aa）	Not recorded	EOH ETHANOL × 2 A1CWM 1-[(3S)-3-amino-2,3-dihydro-1H-indol-1-yl]-3-phenylpropan-1-one × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；292.15 K；PEGII C9: 0.1 M TRIS pH 8.5, 0.2 M magnesium chloride, & 16 % PEG 4000	Resolution 1.76 Å R-free 0.240
9YG1 Targeting PTPN22 at non-orthosteric binding sites - a fragment approach Deposited 2025-09-27	Different construct 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 1–303（303 aa）	Not recorded	EOH ETHANOL × 3 A1CWL 1-phenyl-1H-pyrazol-4-ol × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；292.15 K；PEGII C9: 0.1 M TRIS pH 8.5, 0.2 M magnesium chloride, & 16% PEG 4000	Resolution 1.97 Å R-free 0.224
9YG1 Targeting PTPN22 at non-orthosteric binding sites - a fragment approach Deposited 2025-09-27	Different construct 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 1–303（303 aa）	Not recorded	EOH ETHANOL × 4 SO4 SULFATE ION × 1 GOL GLYCEROL × 1 MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；292.15 K；PEGII C9: 0.1 M TRIS pH 8.5, 0.2 M magnesium chloride, & 16% PEG 4000	Resolution 1.97 Å R-free 0.224
9YG2 Targeting PTPN22 at non-orthosteric binding sites - a fragment approach Deposited 2025-09-27	Different construct 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 1–303（303 aa）	Not recorded	CL CHLORIDE ION × 3 EDO 1,2-ETHANEDIOL × 4 GOL GLYCEROL × 1 A1CWK 5-chloro-3-methyl-1-[(3R)-pyrrolidin-3-yl]-1H-indole × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；292.15 K；PTPN22-PD303 (20mg/ml), PEGII C9: 0.1 M TRIS pH 8.5, 0.2 M MgCl2, & 16 % PEG 4000	Resolution 2.26 Å R-free 0.242
9YG2 Targeting PTPN22 at non-orthosteric binding sites - a fragment approach Deposited 2025-09-27	Different construct 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 1–303（303 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 1 GOL GLYCEROL × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；292.15 K；PTPN22-PD303 (20mg/ml), PEGII C9: 0.1 M TRIS pH 8.5, 0.2 M MgCl2, & 16 % PEG 4000	Resolution 2.26 Å R-free 0.242
9YG3 Targeting PTPN22 at non-orthosteric binding sites - a fragment approach Deposited 2025-09-27	Different construct 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 1–303（303 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 1 NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；292.15 K；0.2M MgCl2, 25.00%w/v PEG 3350, 0.10M HEPES, pH 7.5	Resolution 1.96 Å R-free 0.241
9YG3 Targeting PTPN22 at non-orthosteric binding sites - a fragment approach Deposited 2025-09-27	Different construct 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 1–303（303 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 1 NA SODIUM ION × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；292.15 K；0.2M MgCl2, 25.00%w/v PEG 3350, 0.10M HEPES, pH 7.5	Resolution 1.96 Å R-free 0.241

13 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	PTN22_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–21； UniProt 787–807

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	7aam
Deposition date deposition_date	2020-09-04
Structure title title	Crystal structure of the F-BAR domain of PSTIPIP1 bound to the CTH domain of the phosphatase LYP
Keywords keywords	pyogenic arthritis, pyoderma gangrenosum and acne (PAPA), Inflammatory response, membrane binding, SIGNALING PROTEIN; SIGNALING 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	49.30 Å
Radius of gyration Rg (electron density) rg_electron	51.88 Å
Forward intensity I(0) i0	77684100.00
Molecular weight molecular_weight	67619.0 kDa
Excluded volume excluded_volume	83245 Å³
Envelope volume envelope_volume	115740 Å³
Hydration-shell volume shell_volume	26037 Å³
Envelope diameter envelope_diameter	221.8 Å
Shell Rg shell_rg	36.31 Å
Envelope Rg envelope_rg	55.05 Å
Shape Rg shape_rg	51.98 Å
Total Rg total_rg	50.74 Å
Total atoms total_atoms	4745
Residues n_residues	586
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	226.1 Å
Rg (real space) rg_real	51.79 Å
Rg uncertainty (real space) rg_real_error	5.09 Å
I(0) (real space) i0_real	7.7680e+07
I(0) uncertainty (real space) i0_real_error	1.8250e+06
Rg (reciprocal space) rg_reciprocal	49.32 Å
I(0) (reciprocal space) i0_reciprocal	77430000.0000
Solution quality estimate total_estimate	0.6074
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	28.3 Å
Skewness Skewness skewness	0.878
Kurtosis Kurtosis kurtosis	0.247
Angular range angular_range	— – 0.1600 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2144000.0000
Real-space data points n_real_points	33
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.004; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.001; Smooth: 0.886

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Proline-serine-threonine phosphatase-interacting protein 1
Molecular weight formula_weight	34260.5 kDa
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	4925

GSHMMPQLQFKDAFWCRDFTAHTGYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQTEINSLRASFDSLKQQMENVGSSHIQLALTLREELRSLEEFRERQKEQRKKYEAVMDRVQKSKLSLYKKAMESKKTYEQKCRDADDAEQAFERISANGHQKQVEKSQNKARQCKDSATEAERVYRQSIAQLEKVRAEWEQEHRTTCEAFQLQEFDRLTILRNALWVHSNQLSMQCVKDDELYEEVRLTLEGCSIDADIDSFIQAKSTGTEPPAPVPYQNYYD

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 2 Entity 2 polymer

Description description	Tyrosine-protein phosphatase non-receptor type 22
Molecular weight formula_weight	2385.7 kDa
EC 编号 ec_number	3.1.3.48
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

GFANRFSKPKGPRNPPPTWNI

Entity 3 Entity 3 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	162

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7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id	7aamA01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1270 — Substrate Binding Domain Of Dnak; Chain:A; Domain 2
Homologous superfamily homologous superfamily	60 — Arfaptin homology (AH) domain/BAR domain

Domain ID domain_id	7aamB01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1270 — Substrate Binding Domain Of Dnak; Chain:A; Domain 2
Homologous superfamily homologous superfamily	60 — Arfaptin homology (AH) domain/BAR domain

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8. Citations (1)

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Unit-cell length a length_a	47.996 Å
Unit-cell length b length_b	72.037 Å
Unit-cell length c length_c	205.034 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	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	orthorhombic

Resolution resolution	2.150 Å
Low-resolution limit resolution_low	102.520 Å
R factor r_factor	0.2068
R_work r_work	0.2049
R_free r_free	0.2409

fit	/app/data/saxs_computation/aa/7aam/7aam.fit
pddf	/app/data/pr_computation/aa/7aam/7aam.pr.out
profile	/app/data/saxs_computation/aa/7aam/7aam.dat

Crystal structure of the F-BAR domain of PSTIPIP1 bound to the CTH domain of the phosphatase LYP

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

Proline-serine-threonine phosphatase-interacting protein 1

State in the Current Structure

Other States of the Same Protein in the Database

Tyrosine-protein phosphatase non-receptor type 22

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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)