4urw

The crystal structure of H-Ras and SOS in complex with ligands

Method: X-RAY DIFFRACTION Dmax: 100.2 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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain R; UniProt 1–166 Fragment:UNP RESIDUES 1-166 SON OF SEVENLESS HOMOLOG 1 × 1 (Q07889) DXO 2-(2,6-DIMETHYLPHENYL)-4-(METHYLSULFANYL)-6-(PIPERAZIN-1-YL)-1,3,5-TRIAZINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:3.2M SODIUM FORMATE, 2% DMSO Resolution 2.76 Å R-free 0.230

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 20–185; 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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain S; UniProt 564–1049 Fragment:UNP RESIDUES 564-1049 GTPASE HRAS × 1 (P01112) DXO 2-(2,6-DIMETHYLPHENYL)-4-(METHYLSULFANYL)-6-(PIPERAZIN-1-YL)-1,3,5-TRIAZINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:3.2M SODIUM FORMATE, 2% DMSO Resolution 2.76 Å R-free 0.230

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 2–487; 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 4urw

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4urw
Deposition date deposition_date2014-07-02
Structure title titleThe crystal structure of H-Ras and SOS in complex with ligands
Keywords keywordsSIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.13
Radius of gyration Rg (electron density) rg_electron28.36
Forward intensity I(0) i082370400.00
Molecular weight molecular_weight72061.0 kDa
Excluded volume excluded_volume90579 ų
Envelope volume envelope_volume112710 ų
Hydration-shell volume shell_volume33673 ų
Envelope diameter envelope_diameter107.1
Shell Rg shell_rg35.07
Envelope Rg envelope_rg28.60
Shape Rg shape_rg28.36
Total Rg total_rg29.04
Total atoms total_atoms5080
Residues n_residues621
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 dmax100.2
Rg (real space) rg_real29.15
Rg uncertainty (real space) rg_real_error0.98
I(0) (real space) i0_real8.2370e+07
I(0) uncertainty (real space) i0_real_error1.3380e+06
Rg (reciprocal space) rg_reciprocal29.15
I(0) (reciprocal space) i0_reciprocal82370000.0000
Solution quality estimate total_estimate0.7977
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary31.6
Skewness Skewness skewness0.380
Kurtosis Kurtosis kurtosis-0.317
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24500000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.800; Stabil: 0.996; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd4urwr1
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_idd4urwr2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4urws_
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 (3 domains)

Domain ID domain_id4urwR00
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_id4urwS01
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_id4urwS02
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)