8qdv

Structure of 14-3-3 zeta delta C with the bivalent tau-pS214-pS324 peptide

Method: X-RAY DIFFRACTION Dmax: 96.8 Å Quality: GOOD

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

14-3-3 protein zeta/delta

Homo sapiens

UniProt P63104

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–230 Chain B; UniProt 1–230 Not recorded Microtubule-associated protein tau × 1 (P10636) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.2M Sodium Fluoride, 0.1M bis-tris propane pH 6.5, 20% w/v PEG 3350 Resolution 2.50 Å R-free 0.260
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 1–230 Chain G; UniProt 1–230 Not recorded Microtubule-associated protein tau × 1 (P10636) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.2M Sodium Fluoride, 0.1M bis-tris propane pH 6.5, 20% w/v PEG 3350 Resolution 2.50 Å R-free 0.260

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.

73 other PDB entries and 87 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name 1433Z_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–230; UniProt 1–230 Author chain B; PDBConstruct 1–230; UniProt 1–230 Author chain E; PDBConstruct 1–230; UniProt 1–230 Author chain G; PDBConstruct 1–230; UniProt 1–230

Microtubule-associated protein tau

OrganismNot specified

UniProt P10636

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 527–539 Chain C; UniProt 635–648 Non-standard monomer:Yes (specific site not provided by mmCIF) 14-3-3 protein zeta/delta × 2 (P63104) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.2M Sodium Fluoride, 0.1M bis-tris propane pH 6.5, 20% w/v PEG 3350 Resolution 2.50 Å R-free 0.260
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 527–539 Chain F; UniProt 635–648 Non-standard monomer:Yes (specific site not provided by mmCIF) 14-3-3 protein zeta/delta × 2 (P63104) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.2M Sodium Fluoride, 0.1M bis-tris propane pH 6.5, 20% w/v PEG 3350 Resolution 2.50 Å R-free 0.260

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.

248 other PDB entries and 269 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TAU_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–13; UniProt 527–539 Author chain C; PDBConstruct 25–38; UniProt 635–648 Author chain F; PDBConstruct 1–13; UniProt 527–539 Author chain F; PDBConstruct 25–38; UniProt 635–648

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 8qdv

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8qdv
Deposition date deposition_date2023-08-30
Structure title titleStructure of 14-3-3 zeta delta C with the bivalent tau-pS214-pS324 peptide
Keywords keywords14-3-3 zeta, tau, protein-protein interaction, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier34.68
Radius of gyration Rg (electron density) rg_electron33.70
Forward intensity I(0) i0172769000.00
Molecular weight molecular_weight102880.0 kDa
Excluded volume excluded_volume127980 ų
Envelope volume envelope_volume184070 ų
Hydration-shell volume shell_volume44920 ų
Envelope diameter envelope_diameter94.2
Shell Rg shell_rg41.81
Envelope Rg envelope_rg31.56
Shape Rg shape_rg33.71
Total Rg total_rg34.35
Total atoms total_atoms7225
Residues n_residues940
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 dmax96.8
Rg (real space) rg_real34.40
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real1.7280e+08
I(0) uncertainty (real space) i0_real_error2.6950e+06
Rg (reciprocal space) rg_reciprocal34.58
I(0) (reciprocal space) i0_reciprocal172800000.0000
Solution quality estimate total_estimate0.8898
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary54.7
Skewness Skewness skewness-0.179
Kurtosis Kurtosis kurtosis-0.738
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15430000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.931; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.771

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)