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5w0x

Crystal structure of mouse TOR signaling pathway regulator-like (TIPRL) delta 94-103

Method: X-RAY DIFFRACTION Dmax: 65.2 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

TIP41-like protein

Mus musculus

UniProt Q8BH58

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 12–259 Fragment：UNP residues 12-259 Non-standard monomer：Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6.5；291 K；0.1M Cacodylate pH6.5 15% PEG1000(v/v) 0.2M Magnesium chloride Resolution 2.72 Å R-free 0.273

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 5W0X Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
5W0W Crystal structure of Protein Phosphatase 2A bound to TIPRL Deposited 2017-06-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 12–259（248 aa）
Not recorded MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.2；292 K；0.1M citric acid pH 5.2, 9% PEG4000, 0.2M sodium acetate
Resolution 3.80 Å R-free 0.246
5W0W Crystal structure of Protein Phosphatase 2A bound to TIPRL Deposited 2017-06-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain E 12–259（248 aa）
Not recorded MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.2；292 K；0.1M citric acid pH 5.2, 9% PEG4000, 0.2M sodium acetate
Resolution 3.80 Å R-free 0.246
5W0W Crystal structure of Protein Phosphatase 2A bound to TIPRL Deposited 2017-06-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain H 12–259（248 aa）
Not recorded MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.2；292 K；0.1M citric acid pH 5.2, 9% PEG4000, 0.2M sodium acetate
Resolution 3.80 Å R-free 0.246
5W0W Crystal structure of Protein Phosphatase 2A bound to TIPRL Deposited 2017-06-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain K 12–259（248 aa）
Not recorded MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.2；292 K；0.1M citric acid pH 5.2, 9% PEG4000, 0.2M sodium acetate
Resolution 3.80 Å R-free 0.246

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

View Construct and Data Evidence
UniProt name TIPRL_MOUSE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 3–240； UniProt 12–259

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 5w0x

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5w0x
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5w0x
Deposition date deposition_date2017-06-01
Structure title titleCrystal structure of mouse TOR signaling pathway regulator-like (TIPRL) delta 94-103
Keywords keywordsButterfly-like fold Protein phosphotase 2A regulator, SIGNALING PROTEIN; SIGNALING PROTEIN
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_guinier19.15 Å
Radius of gyration Rg (electron density) rg_electron18.03 Å
Forward intensity I(0) i011449400.00
Molecular weight molecular_weight25100.0 kDa
Excluded volume excluded_volume31273 ų
Envelope volume envelope_volume37365 ų
Hydration-shell volume shell_volume17414 ų
Envelope diameter envelope_diameter66.0 Å
Shell Rg shell_rg24.12 Å
Envelope Rg envelope_rg18.49 Å
Shape Rg shape_rg18.02 Å
Total Rg total_rg19.02 Å
Total atoms total_atoms1741
Residues n_residues206
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 dmax65.2 Å
Rg (real space) rg_real19.08 Å
Rg uncertainty (real space) rg_real_error0.41 Å
I(0) (real space) i0_real1.1450e+07
I(0) uncertainty (real space) i0_real_error1.4630e+05
Rg (reciprocal space) rg_reciprocal19.09 Å
I(0) (reciprocal space) i0_reciprocal11450000.0000
Solution quality estimate total_estimate0.8765
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.6 Å
Skewness Skewness skewness0.245
Kurtosis Kurtosis kurtosis-0.345
Angular range angular_range— – 0.4150 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2987000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.803; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.992
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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8. Citations (1)

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9. Files and Curves (10)