8th6

Crystal Structure of the G3BP1 NTF2-like domain bound to USP10 peptide

Method: X-RAY DIFFRACTION Dmax: 92.4 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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–139 Chain D; UniProt 1–139 Not recorded Ubiquitin carboxyl-terminal hydrolase 10 × 2 (Q14694) EDO 1,2-ETHANEDIOL × 11 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277.15 K;0.1 M HEPES pH 7.5, 25% PEG3350 Resolution 2.34 Å R-free 0.295
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–139 Chain C; UniProt 1–139 Not recorded Ubiquitin carboxyl-terminal hydrolase 10 × 2 (Q14694) EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277.15 K;0.1 M HEPES pH 7.5, 25% PEG3350 Resolution 2.34 Å R-free 0.295

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 28 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

Ubiquitin carboxyl-terminal hydrolase 10

Homo sapiens

UniProt Q14694

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 E; UniProt 2–24 Chain H; UniProt 2–24 Not recorded Ras GTPase-activating protein-binding protein 1 × 2 (Q13283) EDO 1,2-ETHANEDIOL × 11 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277.15 K;0.1 M HEPES pH 7.5, 25% PEG3350 Resolution 2.34 Å R-free 0.295
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 2–24 Chain G; UniProt 2–24 Not recorded Ras GTPase-activating protein-binding protein 1 × 2 (Q13283) EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277.15 K;0.1 M HEPES pH 7.5, 25% PEG3350 Resolution 2.34 Å R-free 0.295

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name UBP10_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 2–24; UniProt 2–24 Author chain F; PDBConstruct 2–24; UniProt 2–24 Author chain G; PDBConstruct 2–24; UniProt 2–24 Author chain H; PDBConstruct 2–24; UniProt 2–24

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 8th6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8th6
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8th6
Deposition date deposition_date2023-07-14
Structure title titleCrystal Structure of the G3BP1 NTF2-like domain bound to USP10 peptide
Keywords keywordsNTF2L USP10, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.57
Radius of gyration Rg (electron density) rg_electron28.55
Forward intensity I(0) i079891100.00
Molecular weight molecular_weight69697.0 kDa
Excluded volume excluded_volume86910 ų
Envelope volume envelope_volume112710 ų
Hydration-shell volume shell_volume32617 ų
Envelope diameter envelope_diameter101.0
Shell Rg shell_rg36.34
Envelope Rg envelope_rg28.30
Shape Rg shape_rg28.51
Total Rg total_rg29.48
Total atoms total_atoms4922
Residues n_residues602
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 dmax92.4
Rg (real space) rg_real29.50
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real7.9890e+07
I(0) uncertainty (real space) i0_real_error1.2180e+06
Rg (reciprocal space) rg_reciprocal29.54
I(0) (reciprocal space) i0_reciprocal79890000.0000
Solution quality estimate total_estimate0.9118
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary90.7
Skewness Skewness skewness0.178
Kurtosis Kurtosis kurtosis-0.686
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha30530000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.952; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)