6s9k

Structure of 14-3-3 gamma in complex with caspase-2 peptide containing 14-3-3 binding motif Ser139 and NLS

Method: X-RAY DIFFRACTION Dmax: 66.2 Å Quality: REASONABLE

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 Mutation:none Caspase-2 × 2 (P42575) CFH 1,1,1,3,3,3-hexafluoropropan-2-ol × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293.15 K;PEG 400, calcium chloride, HEPES, 1,1,1,3,3,3-hexafluoropropan-2-ol Resolution 1.60 Å R-free 0.221

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 1–234; UniProt 1–234

Caspase-2

OrganismNot specified

UniProt P42575

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 B; UniProt 135–168 Non-standard monomer:Yes (specific site not provided by mmCIF) 14-3-3 protein gamma × 2 (P61981) CFH 1,1,1,3,3,3-hexafluoropropan-2-ol × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293.15 K;PEG 400, calcium chloride, HEPES, 1,1,1,3,3,3-hexafluoropropan-2-ol Resolution 1.60 Å R-free 0.221

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.

12 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CASP2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–34; UniProt 135–168

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 6s9k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6s9k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6s9k
Deposition date deposition_date2019-07-15
Structure title titleStructure of 14-3-3 gamma in complex with caspase-2 peptide containing 14-3-3 binding motif Ser139 and NLS
Keywords keywords14-3-3, caspase-2, phosphorylation, NLS, 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_guinier19.24
Radius of gyration Rg (electron density) rg_electron18.28
Forward intensity I(0) i014957800.00
Molecular weight molecular_weight28427.0 kDa
Excluded volume excluded_volume35294 ų
Envelope volume envelope_volume40959 ų
Hydration-shell volume shell_volume18773 ų
Envelope diameter envelope_diameter70.0
Shell Rg shell_rg24.53
Envelope Rg envelope_rg18.72
Shape Rg shape_rg18.28
Total Rg total_rg19.19
Total atoms total_atoms1992
Residues n_residues249
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 dmax66.2
Rg (real space) rg_real19.16
Rg uncertainty (real space) rg_real_error0.25
I(0) (real space) i0_real1.4960e+07
I(0) uncertainty (real space) i0_real_error1.7070e+05
Rg (reciprocal space) rg_reciprocal19.16
I(0) (reciprocal space) i0_reciprocal14960000.0000
Solution quality estimate total_estimate0.6339
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.9
Skewness Skewness skewness0.248
Kurtosis Kurtosis kurtosis-0.207
Angular range angular_range— – 0.4150 −1
Current regularization parameter α current_alpha0.0886
Highest regularization parameter α highest_alpha3555000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.748; Stabil: 1.000; Sysdev: 0.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id6s9kA00
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)