6y4k

Crystal structure of human 14-3-3 gamma in complex with CaMKK2 14-3-3 binding motif Ser100 and Fusicoccin A

Method: X-RAY DIFFRACTION Dmax: 83.6 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 Not recorded Calcium/calmodulin-dependent protein kinase kinase 2 × 2 (Q96RR4) FSC FUSICOCCIN × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;291 K;PEG400, HEPES, magnesium chloride, hexafluoropropanol Resolution 3.00 Å R-free 0.292

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 3–236; UniProt 1–234 Author chain B; 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 97–104 Chain F; UniProt 97–104 Non-standard monomer:Yes (specific site not provided by mmCIF) 14-3-3 protein gamma × 2 (P61981) FSC FUSICOCCIN × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;291 K;PEG400, HEPES, magnesium chloride, hexafluoropropanol Resolution 3.00 Å R-free 0.292

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 25 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 97–104 Author chain F; PDBConstruct 1–8; UniProt 97–104

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 6y4k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6y4k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6y4k
Deposition date deposition_date2020-02-21
Structure title titleCrystal structure of human 14-3-3 gamma in complex with CaMKK2 14-3-3 binding motif Ser100 and Fusicoccin A
Keywords keywords14-3-3 protein, complex, CaMKK, 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_guinier26.97
Radius of gyration Rg (electron density) rg_electron26.17
Forward intensity I(0) i043294900.00
Molecular weight molecular_weight50203.0 kDa
Excluded volume excluded_volume62366 ų
Envelope volume envelope_volume78222 ų
Hydration-shell volume shell_volume25268 ų
Envelope diameter envelope_diameter87.6
Shell Rg shell_rg33.06
Envelope Rg envelope_rg25.86
Shape Rg shape_rg26.22
Total Rg total_rg26.76
Total atoms total_atoms3530
Residues n_residues455
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 dmax83.6
Rg (real space) rg_real27.00
Rg uncertainty (real space) rg_real_error0.61
I(0) (real space) i0_real4.3290e+07
I(0) uncertainty (real space) i0_real_error6.7900e+05
Rg (reciprocal space) rg_reciprocal26.99
I(0) (reciprocal space) i0_reciprocal43290000.0000
Solution quality estimate total_estimate0.8829
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.9
Skewness Skewness skewness0.283
Kurtosis Kurtosis kurtosis-0.643
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10130000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.961; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.943; Smooth: 0.649

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_id6y4kA01
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_id6y4kB01
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)