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1c8z

C-TERMINAL DOMAIN OF MOUSE BRAIN TUBBY PROTEIN

Method: X-RAY DIFFRACTION Dmax: 67.4 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 241–505 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

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 1C8Z Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1I7E C-Terminal Domain Of Mouse Brain Tubby Protein bound to Phosphatidylinositol 4,5-bis-phosphate Deposited 2001-03-08 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 243–505（263 aa） Fragment：C-TERMINAL DOMAIN
Not recorded 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

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 1–265； UniProt 241–505

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 1c8z

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1c8z
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1c8z
Deposition date deposition_date1999-07-30
Structure title titleC-TERMINAL DOMAIN OF MOUSE BRAIN TUBBY PROTEIN
Keywords keywords;TUBBY FILLED-BARREL, BETA-BARREL, FILLED-BETA-ROLL, 12-STRANDED-BETA-BARREL, HELIX-FILLED-BARREL, OBESITY BLINDNESS, DEAFNESS, 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_guinier19.80 Å
Radius of gyration Rg (electron density) rg_electron18.33 Å
Forward intensity I(0) i016630000.00
Molecular weight molecular_weight29567.0 kDa
Excluded volume excluded_volume36620 ų
Envelope volume envelope_volume44156 ų
Hydration-shell volume shell_volume19887 ų
Envelope diameter envelope_diameter69.4 Å
Shell Rg shell_rg24.97 Å
Envelope Rg envelope_rg18.78 Å
Shape Rg shape_rg18.33 Å
Total Rg total_rg19.33 Å
Total atoms total_atoms2076
Residues n_residues265
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 dmax67.4 Å
Rg (real space) rg_real19.67 Å
Rg uncertainty (real space) rg_real_error0.65 Å
I(0) (real space) i0_real1.6630e+07
I(0) uncertainty (real space) i0_real_error2.3170e+05
Rg (reciprocal space) rg_reciprocal19.69 Å
I(0) (reciprocal space) i0_reciprocal16630000.0000
Solution quality estimate total_estimate0.7637
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks4
Primary peak position r_peak_primary26.6 Å
Skewness Skewness skewness0.190
Kurtosis Kurtosis kurtosis-0.269
Angular range angular_range— – 0.4000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3557000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.658; Stabil: 0.983; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; 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_idd1c8za_
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_id1c8zA00
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 (1)

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9. Files and Curves (10)