6v9l

Expanding the Chemical Landscape of SOS1 Activators Using Fragment Based Methods

Method: X-RAY DIFFRACTION Dmax: 114.5 Å Quality: GOOD

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 A; UniProt 1–166 Chain C; UniProt 1–166 Mutation:Y64A Non-standard monomer:Yes (specific site not provided by mmCIF) Son of sevenless homolog 1 × 1 (Q07889) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 ACT ACETATE ION × 1 QTJ 4-(3-chloro-4-fluorophenoxy)benzene-1-sulfonamide × 1 FMT FORMIC ACID × 6 GOL GLYCEROL × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4;293 K;0.1 M sodium acetate, 2.0 M sodium formate, pH 4.0 Resolution 1.70 Å R-free 0.175

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, 3
Chains and sequence ranges Author chain A; PDBConstruct 2–167; UniProt 1–166 Author chain C; PDBConstruct 2–167; 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 B; UniProt 566–1046 Not recorded GTPase HRas × 1 (P01112) GTPase HRas × 1 (P01112) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 ACT ACETATE ION × 1 QTJ 4-(3-chloro-4-fluorophenoxy)benzene-1-sulfonamide × 1 FMT FORMIC ACID × 6 GOL GLYCEROL × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4;293 K;0.1 M sodium acetate, 2.0 M sodium formate, pH 4.0 Resolution 1.70 Å R-free 0.175

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 B; PDBConstruct 2–482; UniProt 566–1046

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 6v9l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6v9l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6v9l
Deposition date deposition_date2019-12-13
Structure title titleExpanding the Chemical Landscape of SOS1 Activators Using Fragment Based Methods
Keywords keywordsRas, SOS, inhibitor, ONCOPROTEIN, Protein-protein complex, MAPK, 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_guinier31.45
Radius of gyration Rg (electron density) rg_electron30.57
Forward intensity I(0) i0142009000.00
Molecular weight molecular_weight94168.0 kDa
Excluded volume excluded_volume117670 ų
Envelope volume envelope_volume145520 ų
Hydration-shell volume shell_volume39629 ų
Envelope diameter envelope_diameter121.1
Shell Rg shell_rg37.65
Envelope Rg envelope_rg30.81
Shape Rg shape_rg30.57
Total Rg total_rg31.18
Total atoms total_atoms6621
Residues n_residues801
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 dmax114.5
Rg (real space) rg_real31.46
Rg uncertainty (real space) rg_real_error1.05
I(0) (real space) i0_real1.4200e+08
I(0) uncertainty (real space) i0_real_error2.3310e+06
Rg (reciprocal space) rg_reciprocal31.46
I(0) (reciprocal space) i0_reciprocal142000000.0000
Solution quality estimate total_estimate0.8531
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.3
Skewness Skewness skewness0.378
Kurtosis Kurtosis kurtosis-0.224
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha41290000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.713; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.959; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (5 domains)

Domain ID domain_idd6v9la_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins
Domain ID domain_idd6v9lb1
Class classa — All alpha proteins
Fold Fold folda.117 — Ras GEF
Superfamily Superfamily superfamilya.117.1 — Ras GEF
Family Family familya.117.1.1 — Ras GEF
Domain ID domain_idd6v9lb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd6v9lc1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins
Domain ID domain_idd6v9lc2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id6v9lC01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

8. Citations (1)

9. Files and Curves (10)