6gkf

Structure of 14-3-3 gamma in complex with caspase-2 14-3-3 binding motif Ser139

Method: X-RAY DIFFRACTION Dmax: 141.0 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 B; UniProt 1–234 Mutation:S235Stop Caspase-2 × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 8.5;293.15 K;PEG 4000, TRIS-HCl, sodium acetate Resolution 2.60 Å R-free 0.289
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–234 Chain D; UniProt 1–234 Mutation:S235Stop Caspase-2 × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 8.5;293.15 K;PEG 4000, TRIS-HCl, sodium acetate Resolution 2.60 Å R-free 0.289
3 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; 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;PEG 4000, TRIS-HCl, sodium acetate Resolution 2.60 Å R-free 0.289
4 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain G; UniProt 1–234 Chain H; UniProt 1–234 Mutation:S235Stop Caspase-2 × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 8.5;293.15 K;PEG 4000, TRIS-HCl, sodium acetate Resolution 2.60 Å R-free 0.289

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 6gkf

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6gkf
Deposition date deposition_date2018-05-20
Structure title titleStructure of 14-3-3 gamma in complex with caspase-2 14-3-3 binding motif Ser139
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_guinier44.36
Radius of gyration Rg (electron density) rg_electron43.93
Forward intensity I(0) i0620139000.00
Molecular weight molecular_weight198890.0 kDa
Excluded volume excluded_volume246140 ų
Envelope volume envelope_volume356980 ų
Hydration-shell volume shell_volume67279 ų
Envelope diameter envelope_diameter146.0
Shell Rg shell_rg49.10
Envelope Rg envelope_rg43.01
Shape Rg shape_rg43.96
Total Rg total_rg44.06
Total atoms total_atoms13994
Residues n_residues1839
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 dmax141.0
Rg (real space) rg_real44.29
Rg uncertainty (real space) rg_real_error1.30
I(0) (real space) i0_real6.2010e+08
I(0) uncertainty (real space) i0_real_error1.1340e+07
Rg (reciprocal space) rg_reciprocal44.36
I(0) (reciprocal space) i0_reciprocal620200000.0000
Solution quality estimate total_estimate0.8913
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary50.9
Skewness Skewness skewness0.240
Kurtosis Kurtosis kurtosis-0.551
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha41510000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.939; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.766

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id6gkfA00
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_id6gkfB00
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_id6gkfC00
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_id6gkfD00
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_id6gkfE00
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_id6gkfF00
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_id6gkfG00
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_id6gkfH00
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)