2b05

Crystal Structure of 14-3-3 gamma in complex with a phosphoserine peptide

Method: X-RAY DIFFRACTION Dmax: 155.3 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 1–246 Chain D; UniProt 1–246 Not recorded peptide × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;PEG 3350, magnesium chloride, Bis-Tris, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.55 Å R-free 0.302
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–246 Chain C; UniProt 1–246 Not recorded peptide × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;PEG 3350, magnesium chloride, Bis-Tris, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.55 Å R-free 0.302
3 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 1–246 Chain F; UniProt 1–246 Not recorded peptide × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;PEG 3350, magnesium chloride, Bis-Tris, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.55 Å R-free 0.302
4 Protein heterocomplex Heteromer Protein × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain A; UniProt 1–246 Chain B; UniProt 1–246 Chain C; UniProt 1–246 Chain D; UniProt 1–246 Chain E; UniProt 1–246 Chain F; UniProt 1–246 Not recorded peptide × 12 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;PEG 3350, magnesium chloride, Bis-Tris, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.55 Å R-free 0.302

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 49 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 1–246 Author chain B; PDBConstruct 1–246; UniProt 1–246 Author chain C; PDBConstruct 1–246; UniProt 1–246 Author chain D; PDBConstruct 1–246; UniProt 1–246 Author chain E; PDBConstruct 1–246; UniProt 1–246 Author chain F; PDBConstruct 1–246; UniProt 1–246

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 2b05

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2b05
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2b05
Deposition date deposition_date2005-09-13
Structure title titleCrystal Structure of 14-3-3 gamma in complex with a phosphoserine peptide
Keywords keywordsCELL CYCLE; CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier45.68
Radius of gyration Rg (electron density) rg_electron45.64
Forward intensity I(0) i0373691000.00
Molecular weight molecular_weight155800.0 kDa
Excluded volume excluded_volume193720 ų
Envelope volume envelope_volume296040 ų
Hydration-shell volume shell_volume56268 ų
Envelope diameter envelope_diameter153.6
Shell Rg shell_rg48.30
Envelope Rg envelope_rg43.93
Shape Rg shape_rg45.66
Total Rg total_rg45.69
Total atoms total_atoms10951
Residues n_residues1424
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 dmax155.3
Rg (real space) rg_real45.80
Rg uncertainty (real space) rg_real_error1.49
I(0) (real space) i0_real3.7370e+08
I(0) uncertainty (real space) i0_real_error7.5490e+06
Rg (reciprocal space) rg_reciprocal45.68
I(0) (reciprocal space) i0_reciprocal373600000.0000
Solution quality estimate total_estimate0.8717
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.8
Skewness Skewness skewness0.295
Kurtosis Kurtosis kurtosis-0.636
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18780000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.845; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.907; Smooth: 0.886

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd2b05a_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.7 — 14-3-3 protein
Family Family familya.118.7.1 — 14-3-3 protein
Domain ID domain_idd2b05b_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.7 — 14-3-3 protein
Family Family familya.118.7.1 — 14-3-3 protein
Domain ID domain_idd2b05c_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.7 — 14-3-3 protein
Family Family familya.118.7.1 — 14-3-3 protein
Domain ID domain_idd2b05d_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.7 — 14-3-3 protein
Family Family familya.118.7.1 — 14-3-3 protein
Domain ID domain_idd2b05e_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.7 — 14-3-3 protein
Family Family familya.118.7.1 — 14-3-3 protein
Domain ID domain_idd2b05f_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.7 — 14-3-3 protein
Family Family familya.118.7.1 — 14-3-3 protein

CATH v4.4 (6 domains)

Domain ID domain_id2b05A00
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_id2b05B00
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_id2b05C00
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_id2b05D00
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_id2b05E00
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_id2b05F00
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)