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10ty

Tissue Non-specific Alkaline Phosphatase -S110A bound to PPi with ethylene glycol

Method: X-RAY DIFFRACTION Dmax: 176.2 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Alkaline phosphatase, tissue-nonspecific isozyme

Mus musculus

UniProt P09242

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Homooligomer Protein × 4 其他Polymer 9 PDB declaration: tetrameric（4） Consistent with protein copy count Chain A； UniProt 17–501 Chain B； UniProt 17–501 Chain C； UniProt 17–501 Chain D； UniProt 17–501 Mutation：S110A ;alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ;alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 POP PYROPHOSPHATE 2- × 4 ZN ZINC ION × 4 MG MAGNESIUM ION × 4 CA CALCIUM ION × 4 NA SODIUM ION × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 MAN alpha-D-mannopyranose × 1 PO4 PHOSPHATE ION × 2 FLC CITRATE ANION × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；293.15 K；0.15 M phosphate/citrate pH 4.0, 0.2 M NaCl, 0-30 mM phosphate, 14-16% PEG 10,000 Resolution 2.28 Å R-free 0.249

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 10TY Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
10TV Tissue Non-specific Alkaline Phosphatase -S110A bound to phosphocreatine Deposited 2026-02-09 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: octameric
Chain A 17–501（485 aa）
Chain B 17–501（485 aa）
Chain C 17–501（485 aa）
Chain D 17–501（485 aa）
Mutation：S110A Mutation：S110A Mutation：S110A Mutation：S110A XDC Phosphocreatine × 4 ZN ZINC ION × 4 MG MAGNESIUM ION × 4 CA CALCIUM ION × 4 GOL GLYCEROL × 10 NA SODIUM ION × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 MAN alpha-D-mannopyranose × 1 PO4 PHOSPHATE ION × 3 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 FLC CITRATE ANION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293.15 K；0.15 M phosphate/citrate pH 4.0, 0.2 M NaCl, 0-30 mM phosphate, 5% glycerol, 14-16% PEG 10,000
Resolution 2.26 Å R-free 0.216
10TW Tissue Non-specific Alkaline Phosphatase -D370G bound to phosphocreatine Deposited 2026-02-09 Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 17–501（485 aa）
Chain B 17–501（485 aa）
Chain C 17–501（485 aa）
Chain D 17–501（485 aa）
Mutation：D370G Mutation：D370G Mutation：D370G Mutation：D370G PO4 PHOSPHATE ION × 4 ZN ZINC ION × 4 MG MAGNESIUM ION × 4 CA CALCIUM ION × 4 NA SODIUM ION × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 GOL GLYCEROL × 6 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 FLC CITRATE ANION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293.15 K；0.15 M phosphate/citrate pH 4.0, 0.2 M NaCl, 0-30 mM phosphate, 5% glycerol, 14-16% PEG 10,000
Resolution 2.12 Å R-free 0.216
10TX Tissue Non-specific Alkaline Phosphatase -S110A bound to PPi Deposited 2026-02-09 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 17–501（485 aa）
Chain B 17–501（485 aa）
Chain C 17–501（485 aa）
Chain D 17–501（485 aa）
Mutation：S110A Mutation：S110A Mutation：S110A Mutation：S110A NA SODIUM ION × 4 POP PYROPHOSPHATE 2- × 4 ZN ZINC ION × 4 MG MAGNESIUM ION × 4 CA CALCIUM ION × 4 GOL GLYCEROL × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 PO4 PHOSPHATE ION × 2 FLC CITRATE ANION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293.15 K；0.15 M phosphate/citrate pH 4.0, 0.2 M NaCl, 0-30 mM phosphate, 5% glycerol, 14-16% PEG 10,000
Resolution 2.25 Å R-free 0.232
10TZ Tissue Non-specific Alkaline Phosphatase -S110A bound to ATP Deposited 2026-02-09 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 17–501（485 aa）
Chain B 17–501（485 aa）
Chain C 17–501（485 aa）
Chain D 17–501（485 aa）
Mutation：S110A Mutation：S110A Mutation：S110A Mutation：S110A ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ZN ZINC ION × 4 MG MAGNESIUM ION × 3 CA CALCIUM ION × 4 GOL GLYCEROL × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 FLC CITRATE ANION × 1 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293.15 K；0.15 M phosphate/citrate pH 4.0, 0.2 M NaCl, 0-30 mM phosphate, 5% glycerol, 14-16% PEG 10,000
Resolution 2.71 Å R-free 0.310

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

View Construct and Data Evidence
UniProt name PPBT_MOUSE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 3–487； UniProt 17–501 Author chain B； PDBConstruct 3–487； UniProt 17–501 Author chain C； PDBConstruct 3–487； UniProt 17–501 Author chain D； PDBConstruct 3–487； UniProt 17–501

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 10ty

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 10ty
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2. Structure Basics 2. Structure Basics

Entry ID entry_id10ty
Deposition date deposition_date2026-02-09
Structure title titleTissue Non-specific Alkaline Phosphatase -S110A bound to PPi with ethylene glycol
Keywords keywordsTNAP, 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_guinier52.31 Å
Radius of gyration Rg (electron density) rg_electron53.05 Å
Forward intensity I(0) i0763465000.00
Molecular weight molecular_weight221020.0 kDa
Excluded volume excluded_volume272800 ų
Envelope volume envelope_volume356430 ų
Hydration-shell volume shell_volume59565 ų
Envelope diameter envelope_diameter185.9 Å
Shell Rg shell_rg50.20 Å
Envelope Rg envelope_rg52.99 Å
Shape Rg shape_rg53.05 Å
Total Rg total_rg52.96 Å
Total atoms total_atoms15484
Residues n_residues1921
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 dmax176.2 Å
Rg (real space) rg_real52.92 Å
Rg uncertainty (real space) rg_real_error2.50 Å
I(0) (real space) i0_real7.6350e+08
I(0) uncertainty (real space) i0_real_error1.6940e+07
Rg (reciprocal space) rg_reciprocal51.78 Å
I(0) (reciprocal space) i0_reciprocal762200000.0000
Solution quality estimate total_estimate0.7133
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary35.2 Å
Skewness Skewness skewness0.567
Kurtosis Kurtosis kurtosis-0.528
Angular range angular_range— – 0.1500 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha109700000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.480; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.668; Smooth: 0.161
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (16)

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8. Citations (1)

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9. Files and Curves (10)