9ivr

Cryo-EM structure of the CHIKV nsP3 peptide in complex with the NTF2L domain of G3BP1 (Conformation II)

Method: ELECTRON MICROSCOPY Dmax: 127.5 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 × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain A; UniProt 1–138 Chain B; UniProt 1–138 Chain C; UniProt 1–138 Chain D; UniProt 1–138 Chain E; UniProt 1–138 Chain F; UniProt 1–138 Chain G; UniProt 1–138 Chain H; UniProt 1–138 Chain M; UniProt 1–138 Chain N; UniProt 1–138 Chain O; UniProt 1–138 Chain P; UniProt 1–138 Chain Q; UniProt 1–138 Chain R; UniProt 1–138 Chain S; UniProt 1–138 Chain T; UniProt 1–138 Not recorded Polyprotein P1234 × 8 (A0A0U5KFN5) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 Å

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 Author chain C; PDBConstruct 4–141; UniProt 1–138 Author chain D; PDBConstruct 4–141; UniProt 1–138 Author chain E; PDBConstruct 4–141; UniProt 1–138 Author chain F; PDBConstruct 4–141; UniProt 1–138 Author chain G; PDBConstruct 4–141; UniProt 1–138 Author chain H; PDBConstruct 4–141; UniProt 1–138 Author chain M; PDBConstruct 4–141; UniProt 1–138 Author chain N; PDBConstruct 4–141; UniProt 1–138 Author chain O; PDBConstruct 4–141; UniProt 1–138 Author chain P; PDBConstruct 4–141; UniProt 1–138 Author chain Q; PDBConstruct 4–141; UniProt 1–138 Author chain R; PDBConstruct 4–141; UniProt 1–138 Author chain S; PDBConstruct 4–141; UniProt 1–138 Author chain T; PDBConstruct 4–141; UniProt 1–138

Polyprotein P1234

Chikungunya virus

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 × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain I; UniProt 1801–1844 Chain J; UniProt 1801–1844 Chain K; UniProt 1801–1844 Chain L; UniProt 1801–1844 Chain U; UniProt 1801–1844 Chain V; UniProt 1801–1844 Chain W; UniProt 1801–1844 Chain X; UniProt 1801–1844 Not recorded Ras GTPase-activating protein-binding protein 1 × 16 (Q13283) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 Å

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 I; PDBConstruct 5–48; UniProt 1801–1844 Author chain J; PDBConstruct 5–48; UniProt 1801–1844 Author chain K; PDBConstruct 5–48; UniProt 1801–1844 Author chain L; PDBConstruct 5–48; UniProt 1801–1844 Author chain U; PDBConstruct 5–48; UniProt 1801–1844 Author chain V; PDBConstruct 5–48; UniProt 1801–1844 Author chain W; PDBConstruct 5–48; UniProt 1801–1844 Author chain X; PDBConstruct 5–48; UniProt 1801–1844

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 9ivr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9ivr
Deposition date deposition_date2024-07-24
Structure title titleCryo-EM structure of the CHIKV nsP3 peptide in complex with the NTF2L domain of G3BP1 (Conformation II)
Keywords keywordsChikungunya virus, nsP3, G3BP1, protein-protein interaction., VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier42.16
Radius of gyration Rg (electron density) rg_electron41.42
Forward intensity I(0) i01190060000.00
Molecular weight molecular_weight279880.0 kDa
Excluded volume excluded_volume347750 ų
Envelope volume envelope_volume467820 ų
Hydration-shell volume shell_volume89052 ų
Envelope diameter envelope_diameter125.4
Shell Rg shell_rg51.10
Envelope Rg envelope_rg40.15
Shape Rg shape_rg41.41
Total Rg total_rg41.86
Total atoms total_atoms19752
Residues n_residues2460
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 dmax127.5
Rg (real space) rg_real41.84
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real1.1900e+09
I(0) uncertainty (real space) i0_real_error1.8570e+07
Rg (reciprocal space) rg_reciprocal42.16
I(0) (reciprocal space) i0_reciprocal1190000000.0000
Solution quality estimate total_estimate0.8946
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary58.6
Skewness Skewness skewness-0.020
Kurtosis Kurtosis kurtosis-0.565
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha296200000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.906; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.954; Smooth: 0.955

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)