9put

HRAS complex with UM0152535 compound

Method: X-RAY DIFFRACTION Dmax: 83.5 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 1–166 Not recorded UM0152535 × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.7;293.15 K;0.1 M Bis-Tris, 0.2 M NaCl2, 21 % PEG 3,350 Resolution 2.00 Å R-free 0.233
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–166 Not recorded UM0152535 × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.7;293.15 K;0.1 M Bis-Tris, 0.2 M NaCl2, 21 % PEG 3,350 Resolution 2.00 Å R-free 0.233

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 323 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 2–167; UniProt 1–166 Author chain C; PDBConstruct 2–167; UniProt 1–166

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 9put

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9put
Deposition date deposition_date2025-07-31
Structure title titleHRAS complex with UM0152535 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_guinier23.60
Radius of gyration Rg (electron density) rg_electron22.92
Forward intensity I(0) i037378000.00
Molecular weight molecular_weight40167.0 kDa
Excluded volume excluded_volume46385 ų
Envelope volume envelope_volume59685 ų
Hydration-shell volume shell_volume22386 ų
Envelope diameter envelope_diameter78.8
Shell Rg shell_rg29.19
Envelope Rg envelope_rg23.02
Shape Rg shape_rg22.87
Total Rg total_rg23.72
Total atoms total_atoms4779
Residues n_residues339
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 dmax83.5
Rg (real space) rg_real23.66
Rg uncertainty (real space) rg_real_error0.79
I(0) (real space) i0_real3.7380e+07
I(0) uncertainty (real space) i0_real_error5.2440e+05
Rg (reciprocal space) rg_reciprocal23.65
I(0) (reciprocal space) i0_reciprocal37380000.0000
Solution quality estimate total_estimate0.7567
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.1
Skewness Skewness skewness0.447
Kurtosis Kurtosis kurtosis-0.304
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9952000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.651; Stabil: 0.996; Sysdev: 1.000; Positv: 1.000; Valcen: 0.890; 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)