6ta7

CRYSTAL STRUCTURE OF HUMAN G3BP1-NTF2 IN COMPLEX WITH HUMAN CAPRIN1-DERIVED SOLOMON MOTIF

Method: X-RAY DIFFRACTION Dmax: 131.3 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Ras GTPase-activating protein-binding protein 1

Homo sapiens

UniProt Q13283

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–139 Chain E; UniProt 1–139 Not recorded NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;298 K;0.2M Sodium chloride, 0.1M Tris 8.0, 20% w/v PEG 4000 of the Proplex crystallization screen (Molecular Dimensions) Resolution 1.93 Å R-free 0.252
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–139 Chain F; UniProt 1–139 Not recorded Caprin-1 × 1 (Q14444) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;298 K;0.2M Sodium chloride, 0.1M Tris 8.0, 20% w/v PEG 4000 of the Proplex crystallization screen (Molecular Dimensions) Resolution 1.93 Å R-free 0.252
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–139 Chain D; UniProt 1–139 Not recorded Caprin-1 × 1 (Q14444) NA SODIUM ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;298 K;0.2M Sodium chloride, 0.1M Tris 8.0, 20% w/v PEG 4000 of the Proplex crystallization screen (Molecular Dimensions) Resolution 1.93 Å R-free 0.252

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.

19 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G3BP1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–140; UniProt 1–139 Author chain B; PDBConstruct 2–140; UniProt 1–139 Author chain C; PDBConstruct 2–140; UniProt 1–139 Author chain D; PDBConstruct 2–140; UniProt 1–139 Author chain E; PDBConstruct 2–140; UniProt 1–139 Author chain F; PDBConstruct 2–140; UniProt 1–139

Caprin-1

OrganismNot specified

UniProt Q14444

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain H; UniProt 356–386 Not recorded Ras GTPase-activating protein-binding protein 1 × 2 (Q13283) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;298 K;0.2M Sodium chloride, 0.1M Tris 8.0, 20% w/v PEG 4000 of the Proplex crystallization screen (Molecular Dimensions) Resolution 1.93 Å R-free 0.252
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain G; UniProt 356–386 Not recorded Ras GTPase-activating protein-binding protein 1 × 2 (Q13283) NA SODIUM ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;298 K;0.2M Sodium chloride, 0.1M Tris 8.0, 20% w/v PEG 4000 of the Proplex crystallization screen (Molecular Dimensions) Resolution 1.93 Å R-free 0.252

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.

4 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CAPR1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain G; PDBConstruct 1–31; UniProt 356–386 Author chain H; PDBConstruct 1–31; UniProt 356–386

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 6ta7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6ta7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6ta7
Deposition date deposition_date2019-10-29
Structure title titleCRYSTAL STRUCTURE OF HUMAN G3BP1-NTF2 IN COMPLEX WITH HUMAN CAPRIN1-DERIVED SOLOMON MOTIF
Keywords keywordsStress Granule, Complex, Regulation, Low Complexity Regions, Phase Transition, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier38.73
Radius of gyration Rg (electron density) rg_electron38.66
Forward intensity I(0) i0124096000.00
Molecular weight molecular_weight88198.0 kDa
Excluded volume excluded_volume109460 ų
Envelope volume envelope_volume154350 ų
Hydration-shell volume shell_volume35338 ų
Envelope diameter envelope_diameter133.3
Shell Rg shell_rg41.58
Envelope Rg envelope_rg38.06
Shape Rg shape_rg38.64
Total Rg total_rg38.92
Total atoms total_atoms11859
Residues n_residues791
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 dmax131.3
Rg (real space) rg_real39.07
Rg uncertainty (real space) rg_real_error1.51
I(0) (real space) i0_real1.2410e+08
I(0) uncertainty (real space) i0_real_error2.3830e+06
Rg (reciprocal space) rg_reciprocal38.87
I(0) (reciprocal space) i0_reciprocal124100000.0000
Solution quality estimate total_estimate0.8352
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.8
Skewness Skewness skewness0.395
Kurtosis Kurtosis kurtosis-0.595
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14820000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.807; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.726; Smooth: 0.706

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)