6sad

Structure of 14-3-3 gamma in complex with double phosphorylated caspase-2 peptide on Ser139 and Ser164

Method: X-RAY DIFFRACTION Dmax: 86.8 Å Quality: EXCELLENT

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

14-3-3 protein gamma

Homo sapiens

UniProt P61981

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 1–234 Chain B; UniProt 1–234 Mutation:none Caspase-2 × 1 (P42575) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293.15 K;PEG 400, magnesium chloride, HEPES, 1,1,1,3,3,3-hexafluoropropan-2-ol Resolution 2.75 Å R-free 0.271

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.

21 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name 1433G_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–234; UniProt 1–234 Author chain B; PDBConstruct 1–234; UniProt 1–234

Caspase-2

OrganismNot specified

UniProt P42575

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 135–168 Non-standard monomer:Yes (specific site not provided by mmCIF) 14-3-3 protein gamma × 2 (P61981) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293.15 K;PEG 400, magnesium chloride, HEPES, 1,1,1,3,3,3-hexafluoropropan-2-ol Resolution 2.75 Å R-free 0.271

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.

12 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CASP2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–34; UniProt 135–168

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 6sad

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6sad
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6sad
Deposition date deposition_date2019-07-16
Structure title titleStructure of 14-3-3 gamma in complex with double phosphorylated caspase-2 peptide on Ser139 and Ser164
Keywords keywords14-3-3 protein, caspase-2, complex, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.78
Radius of gyration Rg (electron density) rg_electron26.98
Forward intensity I(0) i050523000.00
Molecular weight molecular_weight53625.0 kDa
Excluded volume excluded_volume66340 ų
Envelope volume envelope_volume85293 ų
Hydration-shell volume shell_volume26656 ų
Envelope diameter envelope_diameter88.7
Shell Rg shell_rg34.07
Envelope Rg envelope_rg26.57
Shape Rg shape_rg27.00
Total Rg total_rg27.63
Total atoms total_atoms3767
Residues n_residues483
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 dmax86.8
Rg (real space) rg_real27.78
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real5.0520e+07
I(0) uncertainty (real space) i0_real_error6.7830e+05
Rg (reciprocal space) rg_reciprocal27.78
I(0) (reciprocal space) i0_reciprocal50520000.0000
Solution quality estimate total_estimate0.9087
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary28.9
Skewness Skewness skewness0.253
Kurtosis Kurtosis kurtosis-0.653
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8068000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.965; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.942

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id6sadA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology190 — Delta-Endotoxin; domain 1
Homologous superfamily homologous superfamily20 — 14-3-3 domain
Domain ID domain_id6sadB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology190 — Delta-Endotoxin; domain 1
Homologous superfamily homologous superfamily20 — 14-3-3 domain

8. Citations (1)

9. Files and Curves (10)