6byl

Structure of 14-3-3 gamma bound to O-GlcNAcylated thr peptide

Method: X-RAY DIFFRACTION Dmax: 150.8 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 2–241 Chain D; UniProt 2–241 Not recorded TSASTTVPVTTATTTTTSTW O-GlcNac peptide × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;29% PEG 4000, 200 mM sodium acetate, 0.1 M Tris pH 8.5 Resolution 3.35 Å R-free 0.285
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 2–241 Chain C; UniProt 2–241 Not recorded TSASTTVPVTTATTTTTSTW O-GlcNac peptide × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;29% PEG 4000, 200 mM sodium acetate, 0.1 M Tris pH 8.5 Resolution 3.35 Å R-free 0.285
3 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 2–241 Chain F; UniProt 2–241 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;29% PEG 4000, 200 mM sodium acetate, 0.1 M Tris pH 8.5 Resolution 3.35 Å R-free 0.285

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 50 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 1–240; UniProt 2–241 Author chain B; PDBConstruct 1–240; UniProt 2–241 Author chain C; PDBConstruct 1–240; UniProt 2–241 Author chain D; PDBConstruct 1–240; UniProt 2–241 Author chain E; PDBConstruct 1–240; UniProt 2–241 Author chain F; PDBConstruct 1–240; UniProt 2–241

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 6byl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6byl
Deposition date deposition_date2017-12-20
Structure title titleStructure of 14-3-3 gamma bound to O-GlcNAcylated thr peptide
Keywords keywords14-3-3, O-glcNAc, PEPTIDE BINDING PROTEIN; PEPTIDE BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier46.01
Radius of gyration Rg (electron density) rg_electron45.87
Forward intensity I(0) i0433612000.00
Molecular weight molecular_weight166440.0 kDa
Excluded volume excluded_volume206440 ų
Envelope volume envelope_volume318460 ų
Hydration-shell volume shell_volume59806 ų
Envelope diameter envelope_diameter154.7
Shell Rg shell_rg48.96
Envelope Rg envelope_rg44.38
Shape Rg shape_rg45.89
Total Rg total_rg45.98
Total atoms total_atoms12854
Residues n_residues1447
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 dmax150.8
Rg (real space) rg_real46.13
Rg uncertainty (real space) rg_real_error1.52
I(0) (real space) i0_real4.3360e+08
I(0) uncertainty (real space) i0_real_error7.9820e+06
Rg (reciprocal space) rg_reciprocal46.01
I(0) (reciprocal space) i0_reciprocal433500000.0000
Solution quality estimate total_estimate0.8639
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.8
Skewness Skewness skewness0.320
Kurtosis Kurtosis kurtosis-0.575
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22190000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.896; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.547

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id6bylA00
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_id6bylB00
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_id6bylC00
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_id6bylD00
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_id6bylE00
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_id6bylF00
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)