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1i7e

C-Terminal Domain Of Mouse Brain Tubby Protein bound to Phosphatidylinositol 4,5-bis-phosphate

Method: X-RAY DIFFRACTION Dmax: 65.5 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

TUBBY PROTEIN

Mus musculus

UniProt P50586

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 243–505 Fragment：C-TERMINAL DOMAIN IBS L-ALPHA-GLYCEROPHOSPHO-D-MYO-INOSITOL-4,5-BIS-PHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；2% PEG 4000, 0.1M Hepes, 4% 2-propanol, 5mM DTT, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 20K Resolution 1.95 Å R-free 0.261

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 1I7E Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1C8Z C-TERMINAL DOMAIN OF MOUSE BRAIN TUBBY PROTEIN Deposited 1999-07-30 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 241–505（265 aa）
Not recorded PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；2% PEG 4000, 0.1M HEPES, 4% 2-PROPANOL, 5MM DTT, pH 7.5, VAPOR DIFFUSION, HANGING DROP at 293K
Resolution 1.90 Å R-free 0.265

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

View Construct and Data Evidence
UniProt name TUB_MOUSE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 3–265； UniProt 243–505

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 1i7e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1i7e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1i7e
Deposition date deposition_date2001-03-08
Structure title titleC-Terminal Domain Of Mouse Brain Tubby Protein bound to Phosphatidylinositol 4,5-bis-phosphate
Keywords keywords;tubby filled-barrel beta-barrel filled-beta-roll 12-stranded-beta-barrel helix-filled-barrel obesity blindness deafness phosphoinositide phosphatidylinositol, 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_guinier19.09 Å
Radius of gyration Rg (electron density) rg_electron17.66 Å
Forward intensity I(0) i013546000.00
Molecular weight molecular_weight26833.0 kDa
Excluded volume excluded_volume33358 ų
Envelope volume envelope_volume39604 ų
Hydration-shell volume shell_volume18579 ų
Envelope diameter envelope_diameter68.9 Å
Shell Rg shell_rg24.11 Å
Envelope Rg envelope_rg18.15 Å
Shape Rg shape_rg17.67 Å
Total Rg total_rg18.66 Å
Total atoms total_atoms1884
Residues n_residues237
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 dmax65.5 Å
Rg (real space) rg_real18.99 Å
Rg uncertainty (real space) rg_real_error0.43 Å
I(0) (real space) i0_real1.3550e+07
I(0) uncertainty (real space) i0_real_error1.7260e+05
Rg (reciprocal space) rg_reciprocal19.00 Å
I(0) (reciprocal space) i0_reciprocal13550000.0000
Solution quality estimate total_estimate0.7814
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary24.6 Å
Skewness Skewness skewness0.233
Kurtosis Kurtosis kurtosis-0.194
Angular range angular_range— – 0.4150 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3220000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.719; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1i7ea_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.23 — Tubby C-terminal domain-like
Superfamily Superfamily superfamilyd.23.1 — Tubby C-terminal domain-like
Family Family familyd.23.1.1 — Transcriptional factor tubby, C-terminal domain

CATH v4.4 (1 domains)

Domain ID domain_id1i7eA00
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology90 — Tubby Protein; Chain A
Homologous superfamily homologous superfamily10 — Tubby Protein; Chain A
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8. Citations (2)

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9. Files and Curves (10)