1xd2

Crystal Structure of a ternary Ras:SOS:Ras*GDP complex

Method: X-RAY DIFFRACTION Dmax: 112.4 Å Quality: GOOD

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 A; UniProt 1–166 Chain B; UniProt 1–166 Fragment:residues 1-166 Mutation:Y64A Fragment:residues 1-166 Son of sevenless protein homolog 1 × 1 (Q07889) MG MAGNESIUM ION × 1 PO4 PHOSPHATE ION × 4 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;Hepes, Na/K phosphate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.70 Å R-free 0.245

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 A; PDBConstruct 1–166; UniProt 1–166 Author chain B; 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 C; UniProt 566–1049 Fragment:residues 566-1049, including Ras guanine nucleotide exchange factor fragment Transforming protein p21/H-Ras-1 × 1 (P01112) Transforming protein p21/H-Ras-1 × 1 (P01112) MG MAGNESIUM ION × 1 PO4 PHOSPHATE ION × 4 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;Hepes, Na/K phosphate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.70 Å R-free 0.245

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 C; PDBConstruct 1–484; UniProt 566–1049

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 1xd2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1xd2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1xd2
Deposition date deposition_date2004-09-03
Structure title titleCrystal Structure of a ternary Ras:SOS:Ras*GDP complex
Keywords keywordsRas:SOS complex, Ras-nucleotide exchange factor complex, 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_guinier31.47
Radius of gyration Rg (electron density) rg_electron30.60
Forward intensity I(0) i0141538000.00
Molecular weight molecular_weight93614.0 kDa
Excluded volume excluded_volume116860 ų
Envelope volume envelope_volume145730 ų
Hydration-shell volume shell_volume39706 ų
Envelope diameter envelope_diameter119.4
Shell Rg shell_rg37.55
Envelope Rg envelope_rg30.79
Shape Rg shape_rg30.59
Total Rg total_rg31.22
Total atoms total_atoms6583
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 dmax112.4
Rg (real space) rg_real31.49
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real1.4150e+08
I(0) uncertainty (real space) i0_real_error2.1740e+06
Rg (reciprocal space) rg_reciprocal31.48
I(0) (reciprocal space) i0_reciprocal141500000.0000
Solution quality estimate total_estimate0.8589
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.0
Skewness Skewness skewness0.382
Kurtosis Kurtosis kurtosis-0.224
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha42630000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.748; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.945

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1xd2a_
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_idd1xd2b_
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_idd1xd2c_
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_id1xd2A00
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_id1xd2B00
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_id1xd2C01
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_id1xd2C02
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)