8v1l

Crystal structure of the NTF2L domain of human G3BP1 in complex with small molecule

Method: X-RAY DIFFRACTION Dmax: 104.3 Å Quality: EXCELLENT

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 C; UniProt 1–139 Not recorded Y9M N-[(2S)-2-fluoro-4,4-dimethylpentanoyl]-3-hydroxy-L-valyl-(betaS)-beta-methyl-L-phenylalanyl-D-alanyl-N-benzyl-N,O-dimethyl-L-homoserinamide × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;0.1 M MES pH 6.5, 15% PEG 550 MME Resolution 2.68 Å R-free 0.395
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–139 Chain D; UniProt 1–139 Not recorded Y9M N-[(2S)-2-fluoro-4,4-dimethylpentanoyl]-3-hydroxy-L-valyl-(betaS)-beta-methyl-L-phenylalanyl-D-alanyl-N-benzyl-N,O-dimethyl-L-homoserinamide × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;0.1 M MES pH 6.5, 15% PEG 550 MME Resolution 2.68 Å R-free 0.395
3 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 1–139 Chain F; UniProt 1–139 Not recorded Y9M N-[(2S)-2-fluoro-4,4-dimethylpentanoyl]-3-hydroxy-L-valyl-(betaS)-beta-methyl-L-phenylalanyl-D-alanyl-N-benzyl-N,O-dimethyl-L-homoserinamide × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;0.1 M MES pH 6.5, 15% PEG 550 MME Resolution 2.68 Å R-free 0.395

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 1–139; UniProt 1–139 Author chain B; PDBConstruct 1–139; UniProt 1–139 Author chain C; PDBConstruct 1–139; UniProt 1–139 Author chain D; PDBConstruct 1–139; UniProt 1–139 Author chain E; PDBConstruct 1–139; UniProt 1–139 Author chain F; PDBConstruct 1–139; UniProt 1–139

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 8v1l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8v1l
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8v1l
Deposition date deposition_date2023-11-20
最后修订 last_revision2024-02-14
Structure title titleCrystal structure of the NTF2L domain of human G3BP1 in complex with small molecule
Keywords keywordsSmall Molecule, complex, NTF2L, G3BP1 FAZ compound, 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_guinier33.37
Radius of gyration Rg (electron density) rg_electron32.62
Forward intensity I(0) i0128130000.00
Molecular weight molecular_weight89988.0 kDa
Excluded volume excluded_volume112290 ų
Envelope volume envelope_volume150270 ų
Hydration-shell volume shell_volume38778 ų
Envelope diameter envelope_diameter105.7
Shell Rg shell_rg39.16
Envelope Rg envelope_rg32.29
Shape Rg shape_rg32.60
Total Rg total_rg33.20
Total atoms total_atoms6360
Residues n_residues776
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 dmax104.3
Rg (real space) rg_real33.29
Rg uncertainty (real space) rg_real_error0.66
I(0) (real space) i0_real1.2810e+08
I(0) uncertainty (real space) i0_real_error1.8930e+06
Rg (reciprocal space) rg_reciprocal33.34
I(0) (reciprocal space) i0_reciprocal128100000.0000
Solution quality estimate total_estimate0.9065
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.6
Skewness Skewness skewness0.143
Kurtosis Kurtosis kurtosis-0.614
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha50630000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.950; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.940

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)