9pu8

HRAS complex with UM0140693 compound

Method: X-RAY DIFFRACTION Dmax: 51.1 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 A; UniProt 1–165 Not recorded UM0140693 × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;Tris Resolution 1.40 Å R-free 0.179

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 A; PDBConstruct 2–166; UniProt 1–165

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 9pu8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9pu8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9pu8
Deposition date deposition_date2025-07-30
Structure title titleHRAS complex with UM0140693 compound
Keywords keywordsGTPase, Inhibitor, Macrocycle, SIGNALING PROTEIN, HYDROLASE-INHIBITOR complex; HYDROLASE/INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.49
Radius of gyration Rg (electron density) rg_electron15.12
Forward intensity I(0) i08350880.00
Molecular weight molecular_weight20680.0 kDa
Excluded volume excluded_volume25644 ų
Envelope volume envelope_volume28153 ų
Hydration-shell volume shell_volume15328 ų
Envelope diameter envelope_diameter51.9
Shell Rg shell_rg21.49
Envelope Rg envelope_rg15.42
Shape Rg shape_rg15.11
Total Rg total_rg16.22
Total atoms total_atoms2854
Residues n_residues171
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 dmax51.1
Rg (real space) rg_real16.33
Rg uncertainty (real space) rg_real_error0.21
I(0) (real space) i0_real8.3510e+06
I(0) uncertainty (real space) i0_real_error8.0960e+04
Rg (reciprocal space) rg_reciprocal16.34
I(0) (reciprocal space) i0_reciprocal8351000.0000
Solution quality estimate total_estimate0.8152
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.6
Skewness Skewness skewness0.012
Kurtosis Kurtosis kurtosis-0.497
Angular range angular_range— – 0.4850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2052000.0000
Real-space data points n_real_points79
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.873; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.975; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)