6gkg

Structure of 14-3-3 gamma in complex with caspase-2 14-3-3 binding motif Ser164

Method: X-RAY DIFFRACTION Dmax: 140.0 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 E; UniProt 1–234 Mutation:S235Stop Caspase-2 × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 8.5;293.15 K;Tris-HCl, PEG 4000, lithium sulfate Resolution 2.85 Å R-free 0.287
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–234 Chain F; UniProt 1–234 Mutation:S235Stop Caspase-2 × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 8.5;293.15 K;Tris-HCl, PEG 4000, lithium sulfate Resolution 2.85 Å R-free 0.287
3 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–234 Chain G; UniProt 1–234 Mutation:S235Stop Caspase-2 × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 8.5;293.15 K;Tris-HCl, PEG 4000, lithium sulfate Resolution 2.85 Å R-free 0.287
4 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–234 Chain H; UniProt 1–234 Mutation:S235Stop No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 8.5;293.15 K;Tris-HCl, PEG 4000, lithium sulfate Resolution 2.85 Å R-free 0.287

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 49 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 Author chain C; PDBConstruct 1–234; UniProt 1–234 Author chain D; PDBConstruct 1–234; UniProt 1–234 Author chain E; PDBConstruct 1–234; UniProt 1–234 Author chain F; PDBConstruct 1–234; UniProt 1–234 Author chain G; PDBConstruct 1–234; UniProt 1–234 Author chain H; PDBConstruct 1–234; 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 6gkg

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6gkg
Deposition date deposition_date2018-05-20
Structure title titleStructure of 14-3-3 gamma in complex with caspase-2 14-3-3 binding motif Ser164
Keywords keywordscomplex, phosphorylation, 14-3-3 protein, caspase-2, 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_guinier44.38
Radius of gyration Rg (electron density) rg_electron43.97
Forward intensity I(0) i0625953000.00
Molecular weight molecular_weight200530.0 kDa
Excluded volume excluded_volume248650 ų
Envelope volume envelope_volume361130 ų
Hydration-shell volume shell_volume68088 ų
Envelope diameter envelope_diameter143.4
Shell Rg shell_rg48.98
Envelope Rg envelope_rg43.05
Shape Rg shape_rg44.00
Total Rg total_rg44.09
Total atoms total_atoms14100
Residues n_residues1833
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 dmax140.0
Rg (real space) rg_real44.31
Rg uncertainty (real space) rg_real_error1.07
I(0) (real space) i0_real6.2600e+08
I(0) uncertainty (real space) i0_real_error1.0460e+07
Rg (reciprocal space) rg_reciprocal44.38
I(0) (reciprocal space) i0_reciprocal626000000.0000
Solution quality estimate total_estimate0.8888
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary50.6
Skewness Skewness skewness0.248
Kurtosis Kurtosis kurtosis-0.554
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha48580000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.943; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.721

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id6gkgA00
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_id6gkgB00
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_id6gkgC00
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_id6gkgD00
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_id6gkgE00
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_id6gkgF00
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_id6gkgG00
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_id6gkgH00
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)