6zc9

Structure of 14-3-3 gamma in complex with Nedd4-2 14-3-3 binding motif Ser448

Method: X-RAY DIFFRACTION Dmax: 97.8 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 C; UniProt 1–234 Mutation:S235Stop E3 ubiquitin-protein ligase NEDD4-like × 2 (Q96PU5) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293.15 K;PEG 400, magnesium chloride, HEPES, hexafluoro-2-propanol Resolution 1.90 Å R-free 0.239
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–234 Chain D; UniProt 1–234 Mutation:S235Stop E3 ubiquitin-protein ligase NEDD4-like × 2 (Q96PU5) CFH 1,1,1,3,3,3-hexafluoropropan-2-ol × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293.15 K;PEG 400, magnesium chloride, HEPES, hexafluoro-2-propanol Resolution 1.90 Å R-free 0.239

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 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

E3 ubiquitin-protein ligase NEDD4-like

OrganismNot specified

UniProt Q96PU5

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 444–453 Chain G; UniProt 444–453 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, HANGING DROP;pH 7.5;293.15 K;PEG 400, magnesium chloride, HEPES, hexafluoro-2-propanol Resolution 1.90 Å R-free 0.239
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 444–453 Chain H; UniProt 444–453 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, HANGING DROP;pH 7.5;293.15 K;PEG 400, magnesium chloride, HEPES, hexafluoro-2-propanol Resolution 1.90 Å R-free 0.239

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.

18 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NED4L_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–10; UniProt 444–453 Author chain F; PDBConstruct 1–10; UniProt 444–453 Author chain G; PDBConstruct 1–10; UniProt 444–453 Author chain H; PDBConstruct 1–10; UniProt 444–453

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 6zc9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6zc9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6zc9
Deposition date deposition_date2020-06-10
Structure title titleStructure of 14-3-3 gamma in complex with Nedd4-2 14-3-3 binding motif Ser448
Keywords keywordsE3 ubiquitin protein ligase, complex, phosphorylation, 14-3-3 protein, 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_guinier32.85
Radius of gyration Rg (electron density) rg_electron31.89
Forward intensity I(0) i0188705000.00
Molecular weight molecular_weight105950.0 kDa
Excluded volume excluded_volume131120 ų
Envelope volume envelope_volume175840 ų
Hydration-shell volume shell_volume45470 ų
Envelope diameter envelope_diameter103.3
Shell Rg shell_rg39.70
Envelope Rg envelope_rg30.82
Shape Rg shape_rg31.91
Total Rg total_rg32.48
Total atoms total_atoms7433
Residues n_residues937
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 dmax97.8
Rg (real space) rg_real32.61
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real1.8870e+08
I(0) uncertainty (real space) i0_real_error2.8560e+06
Rg (reciprocal space) rg_reciprocal32.71
I(0) (reciprocal space) i0_reciprocal188700000.0000
Solution quality estimate total_estimate0.9082
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary44.8
Skewness Skewness skewness0.061
Kurtosis Kurtosis kurtosis-0.574
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha20730000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.967; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.916

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id6zc9A01
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_id6zc9B01
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_id6zc9C01
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_id6zc9D01
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)