1nvx

Structural evidence for feedback activation by RasGTP of the Ras-specific nucleotide exchange factor SOS

Method: X-RAY DIFFRACTION Dmax: 98.0 Å Quality: EXCELLENT

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

Transforming protein p21/H-RAS-1

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 Fragment:RESIDUES 1-166 Mutation:A59G Son of sevenless protein homolog 1 × 1 (Q07889) MG MAGNESIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;2-8% PEG 4000, 100 mM MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.20 Å R-free 0.261

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 Q; PDBConstruct 1–166; UniProt 1–166 Author chain R; PDBConstruct 1–166; UniProt 1–166

Son of sevenless protein 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 Fragment:residues 566-10466, including the RAS GUANINE NUCLEOTIDE EXCHANGE FACTOR FRAGMENT Transforming protein p21/H-RAS-1 × 2 (P01112) MG MAGNESIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;2-8% PEG 4000, 100 mM MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.20 Å R-free 0.261

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 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 1nvx

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1nvx
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1nvx
Deposition date deposition_date2003-02-04
Structure title titleStructural evidence for feedback activation by RasGTP of the Ras-specific nucleotide exchange factor SOS
Keywords keywordsProto-oncogene, GTP-binding, Guanine-nucleotide releasing factor, 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_guinier30.67
Radius of gyration Rg (electron density) rg_electron29.77
Forward intensity I(0) i0133263000.00
Molecular weight molecular_weight91215.0 kDa
Excluded volume excluded_volume114120 ų
Envelope volume envelope_volume140950 ų
Hydration-shell volume shell_volume39108 ų
Envelope diameter envelope_diameter103.1
Shell Rg shell_rg37.24
Envelope Rg envelope_rg29.76
Shape Rg shape_rg29.77
Total Rg total_rg30.46
Total atoms total_atoms6418
Residues n_residues780
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 dmax98.0
Rg (real space) rg_real30.61
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real1.3330e+08
I(0) uncertainty (real space) i0_real_error1.9490e+06
Rg (reciprocal space) rg_reciprocal30.64
I(0) (reciprocal space) i0_reciprocal133300000.0000
Solution quality estimate total_estimate0.9036
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.9
Skewness Skewness skewness0.262
Kurtosis Kurtosis kurtosis-0.509
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha38460000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.925; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.968

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1nvxq_
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_idd1nvxr_
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_idd1nvxs_
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

CATH v4.4 (4 domains)

Domain ID domain_id1nvxQ00
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_id1nvxR00
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_id1nvxS01
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_id1nvxS02
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)