10dc

H-Ras GTPase R68A bound to GppNHp

Method: X-RAY DIFFRACTION Dmax: 48.8 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–166 Mutation:R68A GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291.15 K;0.2 M Calcium Acetate, 20% w/v PEG 3350, 0.1% N-octyl glucopyranoside Resolution 2.08 Å R-free 0.215

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 1–166; 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 10dc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 10dc
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id10dc
Deposition date deposition_date2026-01-13
Structure title titleH-Ras GTPase R68A bound to GppNHp
Keywords keywordssmall GTPase, Ras GTPase, GTP analog, HYDROLASE, SIGNALING PROTEIN; HYDROLASE, SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.97
Radius of gyration Rg (electron density) rg_electron14.64
Forward intensity I(0) i07003920.00
Molecular weight molecular_weight18305.0 kDa
Excluded volume excluded_volume22475 ų
Envelope volume envelope_volume24716 ų
Hydration-shell volume shell_volume14092 ų
Envelope diameter envelope_diameter48.4
Shell Rg shell_rg20.73
Envelope Rg envelope_rg14.87
Shape Rg shape_rg14.64
Total Rg total_rg15.71
Total atoms total_atoms1280
Residues n_residues162
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 dmax48.8
Rg (real space) rg_real15.83
Rg uncertainty (real space) rg_real_error0.24
I(0) (real space) i0_real7.0040e+06
I(0) uncertainty (real space) i0_real_error7.8230e+04
Rg (reciprocal space) rg_reciprocal15.84
I(0) (reciprocal space) i0_reciprocal7004000.0000
Solution quality estimate total_estimate0.8985
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.0
Skewness Skewness skewness0.009
Kurtosis Kurtosis kurtosis-0.503
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1116000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.901; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)