10tx

Tissue Non-specific Alkaline Phosphatase -S110A bound to PPi

Method: X-RAY DIFFRACTION Dmax: 175.8 Å Quality: SUSPICIOUS

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)-[alpha-D-mannopyranose-(1-6)]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 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 × 6 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

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.

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 10tx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id10tx
Deposition date deposition_date2026-02-09
Structure title titleTissue Non-specific Alkaline Phosphatase -S110A bound to PPi
Keywords keywordsTNAP, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier52.16
Radius of gyration Rg (electron density) rg_electron52.89
Forward intensity I(0) i0760173000.00
Molecular weight molecular_weight220340.0 kDa
Excluded volume excluded_volume271930 ų
Envelope volume envelope_volume352980 ų
Hydration-shell volume shell_volume59180 ų
Envelope diameter envelope_diameter192.0
Shell Rg shell_rg49.98
Envelope Rg envelope_rg52.92
Shape Rg shape_rg52.89
Total Rg total_rg52.80
Total atoms total_atoms15433
Residues n_residues1919
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

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

Maximum dimension Dmax dmax175.8
Rg (real space) rg_real52.77
Rg uncertainty (real space) rg_real_error1.97
I(0) (real space) i0_real7.6020e+08
I(0) uncertainty (real space) i0_real_error1.3610e+07
Rg (reciprocal space) rg_reciprocal51.63
I(0) (reciprocal space) i0_reciprocal759000000.0000
Solution quality estimate total_estimate0.4822
Solution quality rating solution_quality SUSPICIOUS a SUSPICIOUS solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.1
Skewness Skewness skewness0.569
Kurtosis Kurtosis kurtosis-0.524
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha106100000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.475; Stabil: 1.000; Sysdev: 0.007; Positv: 1.000; Valcen: 0.664; Smooth: 0.153

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (14)

8. Citations (1)

9. Files and Curves (10)