8th7

Crystal Structure of the G3BP1 NTF2-like domain bound to the Caprin1 peptide

Method: X-RAY DIFFRACTION Dmax: 66.7 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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–139 Chain B; UniProt 1–139 Not recorded Caprin-1 × 2 (Q14444) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;291.15 K;1.8M tri-ammonium citrate pH 7.0 Resolution 2.88 Å R-free 0.277

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 29 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

Caprin-1

Homo sapiens

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
1 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 360–381 Chain D; UniProt 360–381 Not recorded Ras GTPase-activating protein-binding protein 1 × 2 (Q13283) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;291.15 K;1.8M tri-ammonium citrate pH 7.0 Resolution 2.88 Å R-free 0.277

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 7 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 C; PDBConstruct 1–22; UniProt 360–381 Author chain D; PDBConstruct 1–22; UniProt 360–381

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 8th7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8th7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8th7
Deposition date deposition_date2023-07-14
Structure title titleCrystal Structure of the G3BP1 NTF2-like domain bound to the Caprin1 peptide
Keywords keywordsNTF2L Caprin1, 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_guinier20.52
Radius of gyration Rg (electron density) rg_electron19.18
Forward intensity I(0) i021195000.00
Molecular weight molecular_weight34150.0 kDa
Excluded volume excluded_volume42352 ų
Envelope volume envelope_volume49574 ų
Hydration-shell volume shell_volume21236 ų
Envelope diameter envelope_diameter67.1
Shell Rg shell_rg25.98
Envelope Rg envelope_rg19.63
Shape Rg shape_rg19.12
Total Rg total_rg20.30
Total atoms total_atoms2405
Residues n_residues309
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 dmax66.7
Rg (real space) rg_real20.43
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real2.1190e+07
I(0) uncertainty (real space) i0_real_error2.8860e+05
Rg (reciprocal space) rg_reciprocal20.45
I(0) (reciprocal space) i0_reciprocal21200000.0000
Solution quality estimate total_estimate0.8123
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.1
Skewness Skewness skewness0.229
Kurtosis Kurtosis kurtosis-0.384
Angular range angular_range— – 0.3850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5555000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.852; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)