8be8

Crystal structure of SOS1-HRas-peptidomimetic4

Method: X-RAY DIFFRACTION Dmax: 100.7 Å Quality: REASONABLE

1. Protein Identity and Related Structures Protein Identity & Related Structures

GTPase HRas

Homo sapiens

UniProt P01112

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain R; UniProt 1–166 Not recorded Son of sevenless homolog 1 × 1 (Q07889) SOS1-HRas-peptidomimetic4 × 1 FMT FORMIC ACID × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;sodium formate 3 M, Tris 100mM pH 8.0 Resolution 2.40 Å R-free 0.237

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.

242 other PDB entries and 324 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RASH_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain R; PDBConstruct 21–186; UniProt 1–166

Son of sevenless homolog 1

Homo sapiens

UniProt Q07889

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain S; UniProt 564–1049 Not recorded GTPase HRas × 1 (P01112) SOS1-HRas-peptidomimetic4 × 1 FMT FORMIC ACID × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;sodium formate 3 M, Tris 100mM pH 8.0 Resolution 2.40 Å R-free 0.237

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.

90 other PDB entries and 115 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SOS1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain S; PDBConstruct 22–507; UniProt 564–1049

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 8be8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8be8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8be8
Deposition date deposition_date2022-10-21
Structure title titleCrystal structure of SOS1-HRas-peptidomimetic4
Keywords keywordsComplex, Stabilizer, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.97
Radius of gyration Rg (electron density) rg_electron28.37
Forward intensity I(0) i083019700.00
Molecular weight molecular_weight72437.0 kDa
Excluded volume excluded_volume91120 ų
Envelope volume envelope_volume113010 ų
Hydration-shell volume shell_volume33703 ų
Envelope diameter envelope_diameter106.8
Shell Rg shell_rg35.08
Envelope Rg envelope_rg28.63
Shape Rg shape_rg28.36
Total Rg total_rg29.09
Total atoms total_atoms5185
Residues n_residues615
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 dmax100.7
Rg (real space) rg_real28.99
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real8.3020e+07
I(0) uncertainty (real space) i0_real_error1.2280e+06
Rg (reciprocal space) rg_reciprocal28.98
I(0) (reciprocal space) i0_reciprocal83020000.0000
Solution quality estimate total_estimate0.6722
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary31.1
Skewness Skewness skewness0.383
Kurtosis Kurtosis kurtosis-0.332
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha27760000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.789; Stabil: 1.000; Sysdev: 0.156; Positv: 1.000; Valcen: 0.907; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)