8xi3

Structure of mouse SCMC-14-3-3gama complex

Method: ELECTRON MICROSCOPY Dmax: 126.3 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

14-3-3 protein gamma

Mus musculus

UniProt P61982

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 1–247 Chain F; UniProt 1–247 Not recorded NACHT, LRR and PYD domains-containing protein 5 × 1 (Q9R1M5) Transducin-like enhancer protein 6 × 1 (Q9WVB3) Oocyte-expressed protein homolog × 1 (Q9CWE6) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 Å

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name 1433G_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain D; PDBConstruct 1–247; UniProt 1–247 Author chain F; PDBConstruct 1–247; UniProt 1–247

NACHT, LRR and PYD domains-containing protein 5

Mus musculus

UniProt Q9R1M5

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 105–1163 Not recorded 14-3-3 protein gamma × 2 (P61982) Transducin-like enhancer protein 6 × 1 (Q9WVB3) Oocyte-expressed protein homolog × 1 (Q9CWE6) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 Å

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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NALP5_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–1059; UniProt 105–1163

Transducin-like enhancer protein 6

Mus musculus

UniProt Q9WVB3

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 48–581 Non-standard monomer:Yes (specific site not provided by mmCIF) 14-3-3 protein gamma × 2 (P61982) NACHT, LRR and PYD domains-containing protein 5 × 1 (Q9R1M5) Oocyte-expressed protein homolog × 1 (Q9CWE6) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 Å

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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TLE6_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain B; PDBConstruct 21–554; UniProt 48–581

Oocyte-expressed protein homolog

Mus musculus

UniProt Q9CWE6

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 1–164 Not recorded 14-3-3 protein gamma × 2 (P61982) NACHT, LRR and PYD domains-containing protein 5 × 1 (Q9R1M5) Transducin-like enhancer protein 6 × 1 (Q9WVB3) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 Å

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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name OOEP_MOUSE
Isoform
PDB entities 4
Chains and sequence ranges Author chain C; PDBConstruct 1–164; UniProt 1–164

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 8xi3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8xi3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8xi3
Deposition date deposition_date2023-12-19
Structure title titleStructure of mouse SCMC-14-3-3gama complex
Keywords keywordsComplex, Oocyte subcortical, phosphorylation, 14-3-3, CYTOSOLIC PROTEIN; CYTOSOLIC PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.60
Radius of gyration Rg (electron density) rg_electron40.94
Forward intensity I(0) i0694140000.00
Molecular weight molecular_weight216240.0 kDa
Excluded volume excluded_volume270730 ų
Envelope volume envelope_volume375020 ų
Hydration-shell volume shell_volume73887 ų
Envelope diameter envelope_diameter126.1
Shell Rg shell_rg48.66
Envelope Rg envelope_rg40.05
Shape Rg shape_rg40.92
Total Rg total_rg41.39
Total atoms total_atoms15157
Residues n_residues1909
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 dmax126.3
Rg (real space) rg_real41.37
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real6.9410e+08
I(0) uncertainty (real space) i0_real_error1.1370e+07
Rg (reciprocal space) rg_reciprocal41.60
I(0) (reciprocal space) i0_reciprocal694300000.0000
Solution quality estimate total_estimate0.8342
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary53.2
Skewness Skewness skewness0.070
Kurtosis Kurtosis kurtosis-0.585
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha96310000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.954; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)