7a6y

Structure of 14-3-3 gamma in complex with DAPK2 peptide stabilized by FC-A

Method: X-RAY DIFFRACTION Dmax: 130.4 Å Quality: GOOD

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–234 Chain C; UniProt 1–234 Not recorded DAPK2 C-terminal peptide × 2 FSC FUSICOCCIN × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;290.15 K;HEPES, MgCl2, PEG400, hexafluoro-2-propanol, FC-A Resolution 2.50 Å R-free 0.259
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–234 Chain D; UniProt 1–234 Not recorded DAPK2 C-terminal peptide × 2 FSC FUSICOCCIN × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;290.15 K;HEPES, MgCl2, PEG400, hexafluoro-2-propanol, FC-A Resolution 2.50 Å R-free 0.259

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 51 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 3–236; UniProt 1–234 Author chain B; PDBConstruct 3–236; UniProt 1–234 Author chain C; PDBConstruct 3–236; UniProt 1–234 Author chain D; PDBConstruct 3–236; UniProt 1–234

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 7a6y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7a6y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7a6y
Deposition date deposition_date2020-08-27
Structure title titleStructure of 14-3-3 gamma in complex with DAPK2 peptide stabilized by FC-A
Keywords keywords14-3-3 protein, DAPK2, kinase, complex, phosphorylation, fusicoccin, 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_guinier38.04
Radius of gyration Rg (electron density) rg_electron38.10
Forward intensity I(0) i0178612000.00
Molecular weight molecular_weight105820.0 kDa
Excluded volume excluded_volume131640 ų
Envelope volume envelope_volume179320 ų
Hydration-shell volume shell_volume42266 ų
Envelope diameter envelope_diameter138.0
Shell Rg shell_rg40.69
Envelope Rg envelope_rg37.64
Shape Rg shape_rg38.11
Total Rg total_rg38.26
Total atoms total_atoms7428
Residues n_residues917
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 dmax130.4
Rg (real space) rg_real38.39
Rg uncertainty (real space) rg_real_error1.35
I(0) (real space) i0_real1.7860e+08
I(0) uncertainty (real space) i0_real_error3.7010e+06
Rg (reciprocal space) rg_reciprocal38.18
I(0) (reciprocal space) i0_reciprocal178600000.0000
Solution quality estimate total_estimate0.8400
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary43.5
Skewness Skewness skewness0.539
Kurtosis Kurtosis kurtosis-0.273
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13300000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.735; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.923; Smooth: 0.787

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id7a6yA01
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_id7a6yB01
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_id7a6yC01
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_id7a6yD01
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)