4nym

Approach for Targeting Ras with Small Molecules that Activate SOS-Mediated Nucleotide Exchange

Method: X-RAY DIFFRACTION Dmax: 114.0 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 Q; UniProt 1–166 Chain R; UniProt 1–166 Mutation:Y64A Son of sevenless homolog 1 × 1 (Q07889) MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 RND N-[1-(1H-indol-3-ylmethyl)piperidin-4-yl]-L-tryptophanamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;293 K;0.1 M sodium acetate, 1.8 M sodium formate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 3.55 Å R-free 0.214

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, 2
Chains and sequence ranges Author chain Q; PDBConstruct 1–166; UniProt 1–166 Author chain R; PDBConstruct 1–166; 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 566–1046 Not recorded GTPase HRas × 1 (P01112) GTPase HRas × 1 (P01112) MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 RND N-[1-(1H-indol-3-ylmethyl)piperidin-4-yl]-L-tryptophanamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;293 K;0.1 M sodium acetate, 1.8 M sodium formate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 3.55 Å R-free 0.214

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 3
Chains and sequence ranges Author chain S; PDBConstruct 1–481; 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 4nym

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4nym
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4nym
Deposition date deposition_date2013-12-10
Structure title titleApproach for Targeting Ras with Small Molecules that Activate SOS-Mediated Nucleotide Exchange
Keywords keywordsGTPase, signaling transduction, Raf, RalGDS, PI3K, cytosol, 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_guinier31.53
Radius of gyration Rg (electron density) rg_electron30.68
Forward intensity I(0) i0139839000.00
Molecular weight molecular_weight93712.0 kDa
Excluded volume excluded_volume117290 ų
Envelope volume envelope_volume146810 ų
Hydration-shell volume shell_volume39900 ų
Envelope diameter envelope_diameter122.3
Shell Rg shell_rg37.59
Envelope Rg envelope_rg30.93
Shape Rg shape_rg30.67
Total Rg total_rg31.29
Total atoms total_atoms6597
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 dmax114.0
Rg (real space) rg_real31.54
Rg uncertainty (real space) rg_real_error1.09
I(0) (real space) i0_real1.3980e+08
I(0) uncertainty (real space) i0_real_error2.4080e+06
Rg (reciprocal space) rg_reciprocal31.54
I(0) (reciprocal space) i0_reciprocal139800000.0000
Solution quality estimate total_estimate0.6370
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.2
Skewness Skewness skewness0.376
Kurtosis Kurtosis kurtosis-0.228
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha41180000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.723; Stabil: 1.000; Sysdev: 0.062; Positv: 1.000; Valcen: 0.967; Smooth: 0.954

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id4nymQ00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id4nymR00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id4nymS01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology870 — Son of sevenless (SoS) protein; Chain S, domain 1
Homologous superfamily homologous superfamily10 — Son of sevenless (SoS) protein Chain: S domain 1
Domain ID domain_id4nymS02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology840 — Son of Sevenless (SoS) protein; Chain S, domain 2
Homologous superfamily homologous superfamily10 — Ras guanine-nucleotide exchange factors catalytic domain

8. Citations (1)

9. Files and Curves (10)