6bzd

Structure of 14-3-3 gamma R57E mutant bound to GlcNAcylated peptide

Method: X-RAY DIFFRACTION Dmax: 98.9 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 2–247 Chain B; UniProt 2–247 Mutation:R57E GlcNAcylated peptide × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;25% PEG 4000, 0.2 M MgCl2, 0.1 M Tris pH 8.5, 20% glycerol Resolution 2.67 Å R-free 0.281
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 2–247 Chain D; UniProt 2–247 Mutation:R57E No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;25% PEG 4000, 0.2 M MgCl2, 0.1 M Tris pH 8.5, 20% glycerol Resolution 2.67 Å R-free 0.281

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 1–246; UniProt 2–247 Author chain B; PDBConstruct 1–246; UniProt 2–247 Author chain C; PDBConstruct 1–246; UniProt 2–247 Author chain D; PDBConstruct 1–246; UniProt 2–247

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 6bzd

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6bzd
Deposition date deposition_date2017-12-22
Structure title titleStructure of 14-3-3 gamma R57E mutant bound to GlcNAcylated peptide
Keywords keywordsreader 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_guinier34.39
Radius of gyration Rg (electron density) rg_electron33.31
Forward intensity I(0) i0206023000.00
Molecular weight molecular_weight111170.0 kDa
Excluded volume excluded_volume137900 ų
Envelope volume envelope_volume194060 ų
Hydration-shell volume shell_volume47909 ų
Envelope diameter envelope_diameter101.5
Shell Rg shell_rg41.36
Envelope Rg envelope_rg31.35
Shape Rg shape_rg33.31
Total Rg total_rg33.97
Total atoms total_atoms7806
Residues n_residues967
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 dmax98.9
Rg (real space) rg_real34.10
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real2.0600e+08
I(0) uncertainty (real space) i0_real_error3.0130e+06
Rg (reciprocal space) rg_reciprocal34.28
I(0) (reciprocal space) i0_reciprocal206100000.0000
Solution quality estimate total_estimate0.8954
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary51.6
Skewness Skewness skewness-0.154
Kurtosis Kurtosis kurtosis-0.649
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17940000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.911; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.920

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_id6bzdA00
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_id6bzdB00
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_id6bzdC00
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_id6bzdD00
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)