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2p6x

Crystal structure of human tyrosine phosphatase PTPN22

Method: X-RAY DIFFRACTION Dmax: 99.0 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Tyrosine-protein phosphatase non-receptor type 22

Homo sapiens

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1–302 Fragment：PTPN22, Tyrosine-protein phosphatase catalytic domain 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
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain B； UniProt 1–302 Fragment：PTPN22, Tyrosine-protein phosphatase catalytic domain 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

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 2P6X Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2QCJ Native Structure of Lyp Deposited 2007-06-19 Different construct 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 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 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 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 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 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 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
7AAM Crystal structure of the F-BAR domain of PSTIPIP1 bound to the CTH domain of the phosphatase LYP Deposited 2020-09-04 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain C 787–807（21 aa）
Not recorded 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
9YDM Targeting PTPN22 at non-orthosteric binding sites - a fragment approach Deposited 2025-09-22 Different construct 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 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 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 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 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 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 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 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 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 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 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 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 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PTN22_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–302； UniProt 1–302 Author chain B； PDBConstruct 1–302； UniProt 1–302

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

SAXS profile for 2p6x

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2p6x
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2p6x
Deposition date deposition_date2007-03-19
Structure title titleCrystal structure of human tyrosine phosphatase PTPN22
Keywords keywordsTyrosine phosphatase, Lymphoid phosphatase, PEP, LYP, Structural Genomics, Structural Genomics Consortium, SGC, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier29.55 Å
Radius of gyration Rg (electron density) rg_electron29.15 Å
Forward intensity I(0) i072630600.00
Molecular weight molecular_weight68904.0 kDa
Excluded volume excluded_volume86873 ų
Envelope volume envelope_volume106110 ų
Hydration-shell volume shell_volume31206 ų
Envelope diameter envelope_diameter101.1 Å
Shell Rg shell_rg35.28 Å
Envelope Rg envelope_rg29.45 Å
Shape Rg shape_rg29.16 Å
Total Rg total_rg29.69 Å
Total atoms total_atoms4847
Residues n_residues598
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax99.0 Å
Rg (real space) rg_real29.67 Å
Rg uncertainty (real space) rg_real_error0.90 Å
I(0) (real space) i0_real7.2630e+07
I(0) uncertainty (real space) i0_real_error1.1630e+06
Rg (reciprocal space) rg_reciprocal29.62 Å
I(0) (reciprocal space) i0_reciprocal72630000.0000
Solution quality estimate total_estimate0.8726
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary29.3 Å
Skewness Skewness skewness0.449
Kurtosis Kurtosis kurtosis-0.403
Angular range angular_range— – 0.2700 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22590000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.828; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.931; Smooth: 0.926
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2p6xa1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.45 — (Phosphotyrosine protein) phosphatases II
Superfamily Superfamily superfamilyc.45.1 — (Phosphotyrosine protein) phosphatases II
Family Family familyc.45.1.0 — automated matches
Domain ID domain_idd2p6xa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2p6xb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.45 — (Phosphotyrosine protein) phosphatases II
Superfamily Superfamily superfamilyc.45.1 — (Phosphotyrosine protein) phosphatases II
Family Family familyc.45.1.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id2p6xA00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology190 — Protein-Tyrosine Phosphatase; Chain A
Homologous superfamily homologous superfamily10 — Protein tyrosine phosphatase superfamily
Domain ID domain_id2p6xB00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology190 — Protein-Tyrosine Phosphatase; Chain A
Homologous superfamily homologous superfamily10 — Protein tyrosine phosphatase superfamily
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8. Citations (1)

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9. Files and Curves (10)