9j5s

Crystal structure of human G3BP1 in complex with CHIKV nsP3 peptide

Method: X-RAY DIFFRACTION Dmax: 72.5 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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–138 Chain B; UniProt 1–138 Not recorded Polyprotein P1234 × 2 (A0A0U5KFN5) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4;291 K;20%(w/v) PEG 3350, 200mM Sodium citrate tribasic, 100mM Sodium citrate/Citric acid pH 4.0 Resolution 2.84 Å R-free 0.280

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 4–141; UniProt 1–138 Author chain B; PDBConstruct 4–141; UniProt 1–138

Polyprotein P1234

OrganismNot specified

UniProt A0A0U5KFN5

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 1806–1831 Chain D; UniProt 1806–1831 Not recorded Ras GTPase-activating protein-binding protein 1 × 2 (Q13283) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4;291 K;20%(w/v) PEG 3350, 200mM Sodium citrate tribasic, 100mM Sodium citrate/Citric acid pH 4.0 Resolution 2.84 Å R-free 0.280

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A0U5KFN5_CHIKV
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–26; UniProt 1806–1831 Author chain D; PDBConstruct 1–26; UniProt 1806–1831

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 9j5s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9j5s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9j5s
Deposition date deposition_date2024-08-13
Structure title titleCrystal structure of human G3BP1 in complex with CHIKV nsP3 peptide
Keywords keywordschikungunya virus, non-structural protein, virus-host interaction, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.58
Radius of gyration Rg (electron density) rg_electron19.18
Forward intensity I(0) i019649900.00
Molecular weight molecular_weight32920.0 kDa
Excluded volume excluded_volume40964 ų
Envelope volume envelope_volume49233 ų
Hydration-shell volume shell_volume21067 ų
Envelope diameter envelope_diameter72.6
Shell Rg shell_rg25.99
Envelope Rg envelope_rg19.83
Shape Rg shape_rg19.09
Total Rg total_rg20.40
Total atoms total_atoms2320
Residues n_residues285
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 dmax72.5
Rg (real space) rg_real20.49
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real1.9650e+07
I(0) uncertainty (real space) i0_real_error2.4570e+05
Rg (reciprocal space) rg_reciprocal20.51
I(0) (reciprocal space) i0_reciprocal19650000.0000
Solution quality estimate total_estimate0.8553
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary25.2
Skewness Skewness skewness0.246
Kurtosis Kurtosis kurtosis-0.389
Angular range angular_range— – 0.3850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5836000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.708; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 1.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)