8osm

GTPASE HRAS IN COMPLEX WITH ZN-CYCLEN AT 200 MPA PRESSURE

Method: X-RAY DIFFRACTION Dmax: 48.0 Å Quality: REASONABLE

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 Fragment:GTPase HRAS N-terminally processed GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 PGE TRIETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:BATCH MODE;pH 7.5;293 K;40 MM TRIS HCL, 10 MM MGCL2, 2 MM DTE, 26-30 % PEG-400 Resolution 2.05 Å R-free 0.224

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 8osm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8osm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8osm
Deposition date deposition_date2023-04-19
Structure title titleGTPASE HRAS IN COMPLEX WITH ZN-CYCLEN AT 200 MPA PRESSURE
Keywords keywordsG PROTEIN, SIGNALING PROTEIN, HPMX, ONCOPROTEIN; ONCOPROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.14
Radius of gyration Rg (electron density) rg_electron14.81
Forward intensity I(0) i07897750.00
Molecular weight molecular_weight19542.0 kDa
Excluded volume excluded_volume23988 ų
Envelope volume envelope_volume26283 ų
Hydration-shell volume shell_volume14687 ų
Envelope diameter envelope_diameter47.6
Shell Rg shell_rg21.15
Envelope Rg envelope_rg15.07
Shape Rg shape_rg14.81
Total Rg total_rg15.88
Total atoms total_atoms1366
Residues n_residues166
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 dmax48.0
Rg (real space) rg_real15.99
Rg uncertainty (real space) rg_real_error0.17
I(0) (real space) i0_real7.8980e+06
I(0) uncertainty (real space) i0_real_error7.6410e+04
Rg (reciprocal space) rg_reciprocal16.00
I(0) (reciprocal space) i0_reciprocal7898000.0000
Solution quality estimate total_estimate0.7410
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.4
Skewness Skewness skewness0.011
Kurtosis Kurtosis kurtosis-0.512
Angular range angular_range— – 0.4950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1519000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.931; Stabil: 1.000; Sysdev: 0.302; Positv: 1.000; Valcen: 0.977; Smooth: 0.954

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (2)

9. Files and Curves (10)