6fel

Structure of 14-3-3 gamma in complex with CaMKK2 14-3-3 binding motif Ser511

Method: X-RAY DIFFRACTION Dmax: 97.0 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–234 Chain B; UniProt 1–234 Not recorded Calcium/calmodulin-dependent protein kinase kinase 2 × 2 (Q96RR4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 5.6;291.15 K;sodium citrate, potassium sodium tartrate, and ammonium sulfate Resolution 2.84 Å R-free 0.280
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 Not recorded Calcium/calmodulin-dependent protein kinase kinase 2 × 2 (Q96RR4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 5.6;291.15 K;sodium citrate, potassium sodium tartrate, and ammonium sulfate Resolution 2.84 Å R-free 0.280

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

Calcium/calmodulin-dependent protein kinase kinase 2

OrganismNot specified

UniProt Q96RR4

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 E; UniProt 508–515 Chain F; UniProt 508–515 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;pH 5.6;291.15 K;sodium citrate, potassium sodium tartrate, and ammonium sulfate Resolution 2.84 Å R-free 0.280
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain G; UniProt 508–515 Chain H; UniProt 508–515 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;pH 5.6;291.15 K;sodium citrate, potassium sodium tartrate, and ammonium sulfate Resolution 2.84 Å R-free 0.280

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 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KKCC2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–8; UniProt 508–515 Author chain F; PDBConstruct 1–8; UniProt 508–515 Author chain G; PDBConstruct 1–8; UniProt 508–515 Author chain H; PDBConstruct 1–8; UniProt 508–515

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 6fel

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6fel
Deposition date deposition_date2018-01-02
Structure title titleStructure of 14-3-3 gamma in complex with CaMKK2 14-3-3 binding motif Ser511
Keywords keywords14-3-3 protein, calcium/calmodulin-dependent protein kinase kinase 2, CaMKK2, phosphorylation, 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_guinier32.60
Radius of gyration Rg (electron density) rg_electron31.56
Forward intensity I(0) i0184143000.00
Molecular weight molecular_weight105500.0 kDa
Excluded volume excluded_volume131100 ų
Envelope volume envelope_volume176020 ų
Hydration-shell volume shell_volume45772 ų
Envelope diameter envelope_diameter101.5
Shell Rg shell_rg39.58
Envelope Rg envelope_rg30.48
Shape Rg shape_rg31.57
Total Rg total_rg32.20
Total atoms total_atoms7406
Residues n_residues923
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 dmax97.0
Rg (real space) rg_real32.33
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real1.8410e+08
I(0) uncertainty (real space) i0_real_error2.6080e+06
Rg (reciprocal space) rg_reciprocal32.45
I(0) (reciprocal space) i0_reciprocal184200000.0000
Solution quality estimate total_estimate0.9073
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary45.5
Skewness Skewness skewness0.026
Kurtosis Kurtosis kurtosis-0.568
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24040000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.956; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.939

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id6felA00
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_id6felB00
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_id6felC00
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_id6felD00
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)