7s17

Crystal structure of human G3BP1-NTF2 with three mutations- F15W, F33W, and F124W

Method: X-RAY DIFFRACTION Dmax: 64.5 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 1–138 Chain B; UniProt 1–138 Mutation:F15W, F33W, F124W No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;291 K;20% PEG 8000, 100 mM HEPES Resolution 2.36 Å R-free 0.271

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 2–139; UniProt 1–138 Author chain B; PDBConstruct 2–139; UniProt 1–138

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 7s17

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7s17
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7s17
Deposition date deposition_date2021-09-01
Structure title titleCrystal structure of human G3BP1-NTF2 with three mutations- F15W, F33W, and F124W
Keywords keywordsNTF2-like domain, binding mutant, 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_guinier20.00
Radius of gyration Rg (electron density) rg_electron18.63
Forward intensity I(0) i017568200.00
Molecular weight molecular_weight30947.0 kDa
Excluded volume excluded_volume38479 ų
Envelope volume envelope_volume46013 ų
Hydration-shell volume shell_volume20286 ų
Envelope diameter envelope_diameter69.0
Shell Rg shell_rg25.37
Envelope Rg envelope_rg19.25
Shape Rg shape_rg18.53
Total Rg total_rg19.87
Total atoms total_atoms2181
Residues n_residues267
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 dmax64.5
Rg (real space) rg_real19.92
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real1.7570e+07
I(0) uncertainty (real space) i0_real_error2.4670e+05
Rg (reciprocal space) rg_reciprocal19.93
I(0) (reciprocal space) i0_reciprocal17570000.0000
Solution quality estimate total_estimate0.8088
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary24.9
Skewness Skewness skewness0.230
Kurtosis Kurtosis kurtosis-0.370
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4774000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.840; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)