8we2

14-3-3 zeta complexed with S609 phosphorylated peptide derived from GPIb alpha cytoplasmic domain

Method: X-RAY DIFFRACTION Dmax: 83.7 Å Quality: EXCELLENT

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–245 Chain B; UniProt 1–245 Not recorded S609 phosphorylated peptide × 2 (P07359) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.2M Sodium Acetate, 20% PEG 3350 Resolution 2.11 Å R-free 0.238

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 88 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 2–246; UniProt 1–245 Author chain B; PDBConstruct 2–246; UniProt 1–245

S609 phosphorylated peptide

OrganismNot specified

UniProt P07359

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain Q; UniProt 646–652 Chain R; UniProt 646–652 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;291 K;0.2M Sodium Acetate, 20% PEG 3350 Resolution 2.11 Å R-free 0.238

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.

20 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GP1BA_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain Q; PDBConstruct 1–7; UniProt 646–652 Author chain R; PDBConstruct 1–7; UniProt 646–652

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 8we2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8we2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8we2
Deposition date deposition_date2023-09-16
Structure title title14-3-3 zeta complexed with S609 phosphorylated peptide derived from GPIb alpha cytoplasmic domain
Keywords keywordsComplex, Phosphorylation, BLOOD CLOTTING; BLOOD CLOTTING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.42
Radius of gyration Rg (electron density) rg_electron26.63
Forward intensity I(0) i047696200.00
Molecular weight molecular_weight52823.0 kDa
Excluded volume excluded_volume65800 ų
Envelope volume envelope_volume85372 ų
Hydration-shell volume shell_volume26868 ų
Envelope diameter envelope_diameter90.5
Shell Rg shell_rg33.85
Envelope Rg envelope_rg26.11
Shape Rg shape_rg26.64
Total Rg total_rg27.38
Total atoms total_atoms3705
Residues n_residues463
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 dmax83.7
Rg (real space) rg_real27.37
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real4.7700e+07
I(0) uncertainty (real space) i0_real_error6.1840e+05
Rg (reciprocal space) rg_reciprocal27.39
I(0) (reciprocal space) i0_reciprocal47700000.0000
Solution quality estimate total_estimate0.9168
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.8
Skewness Skewness skewness0.191
Kurtosis Kurtosis kurtosis-0.681
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6333000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.982; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.977

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)