4j6s

14-3-3gamma complexed with the N-terminal sequence of tyrosine hydroxylase (residues 1-43)

Method: X-RAY DIFFRACTION Dmax: 106.3 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 1–247 Chain B; UniProt 1–247 Not recorded N-terminal motif of tyrosine hydroxylase × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.1;283 K;30% PEG 2000 MME, 0.1M Potassium Thiocyanate, pH 7.1, VAPOR DIFFUSION, temperature 283.0K Resolution 3.08 Å R-free 0.254
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–247 Chain D; UniProt 1–247 Not recorded N-terminal motif of tyrosine hydroxylase × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.1;283 K;30% PEG 2000 MME, 0.1M Potassium Thiocyanate, pH 7.1, VAPOR DIFFUSION, temperature 283.0K Resolution 3.08 Å R-free 0.254

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 1–255; UniProt 1–247 Author chain B; PDBConstruct 1–255; UniProt 1–247 Author chain C; PDBConstruct 1–255; UniProt 1–247 Author chain D; PDBConstruct 1–255; UniProt 1–247

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 4j6s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4j6s
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id4j6s
Deposition date deposition_date2013-02-11
Structure title title14-3-3gamma complexed with the N-terminal sequence of tyrosine hydroxylase (residues 1-43)
Keywords keywords;14-3-3 proteins, peptide binding, Dopamine synthesis, signal transduction, regulatory proteins, tyrosine hydroxylase, phosphorylation, hydrolase ;; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier33.35
Radius of gyration Rg (electron density) rg_electron32.49
Forward intensity I(0) i0214237000.00
Molecular weight molecular_weight113600.0 kDa
Excluded volume excluded_volume140780 ų
Envelope volume envelope_volume187450 ų
Hydration-shell volume shell_volume47888 ų
Envelope diameter envelope_diameter112.2
Shell Rg shell_rg39.75
Envelope Rg envelope_rg32.16
Shape Rg shape_rg32.52
Total Rg total_rg32.94
Total atoms total_atoms7970
Residues n_residues986
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 dmax106.3
Rg (real space) rg_real33.23
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real2.1420e+08
I(0) uncertainty (real space) i0_real_error3.2000e+06
Rg (reciprocal space) rg_reciprocal33.30
I(0) (reciprocal space) i0_reciprocal214300000.0000
Solution quality estimate total_estimate0.8893
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary43.0
Skewness Skewness skewness0.192
Kurtosis Kurtosis kurtosis-0.353
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha29810000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.891; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.886

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id4j6sA00
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_id4j6sB00
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_id4j6sC00
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_id4j6sD00
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)