9pun

HRAS complex with UM0148697 compound

Method: X-RAY DIFFRACTION Dmax: 79.3 Å Quality: EXCELLENT

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–166 Not recorded GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.4;293.15 K;0.1 M Tris, 0.2 M MgCl2, 26 % PEG 3,350 Resolution 2.40 Å R-free 0.260
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–166 Not recorded GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.4;293.15 K;0.1 M Tris, 0.2 M MgCl2, 26 % PEG 3,350 Resolution 2.40 Å R-free 0.260
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–166 Not recorded UM0148697 × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.4;293.15 K;0.1 M Tris, 0.2 M MgCl2, 26 % PEG 3,350 Resolution 2.40 Å R-free 0.260

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 322 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 3–168; UniProt 1–166 Author chain B; PDBConstruct 3–168; UniProt 1–166 Author chain C; PDBConstruct 3–168; 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 9pun

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9pun
Deposition date deposition_date2025-07-31
Structure title titleHRAS complex with UM0148697 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_guinier25.43
Radius of gyration Rg (electron density) rg_electron24.41
Forward intensity I(0) i053965300.00
Molecular weight molecular_weight55364.0 kDa
Excluded volume excluded_volume68511 ų
Envelope volume envelope_volume81762 ų
Hydration-shell volume shell_volume28031 ų
Envelope diameter envelope_diameter82.1
Shell Rg shell_rg31.59
Envelope Rg envelope_rg24.35
Shape Rg shape_rg24.34
Total Rg total_rg25.39
Total atoms total_atoms7661
Residues n_residues471
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 dmax79.3
Rg (real space) rg_real25.36
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real5.3970e+07
I(0) uncertainty (real space) i0_real_error7.2990e+05
Rg (reciprocal space) rg_reciprocal25.39
I(0) (reciprocal space) i0_reciprocal53970000.0000
Solution quality estimate total_estimate0.9080
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.2
Skewness Skewness skewness0.249
Kurtosis Kurtosis kurtosis-0.479
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8517000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.945; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.964

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)