8cnj

HRas(1-166) in complex with GDP and BeF3-

Method: X-RAY DIFFRACTION Dmax: 76.9 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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–166 Chain B; UniProt 1–166 Fragment:GTPase HRAS N-terminally processed GDP GUANOSINE-5'-DIPHOSPHATE × 2 BEF BERYLLIUM TRIFLUORIDE ION × 2 MG MAGNESIUM ION × 2 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;BeF3- GSA complexes were obtained under vapour diffusion sitting drop conditions. Protein buffer (HRas pY64 or HRas 0.4 mM, Na-HEPES 20 mM pH = 8.0, MgCl2 5 mM, NaF 20 mM) were mixed with precipitant in a 1:1 ratio with a total drop size of 600 nL. The precipitant solution consited of: (30 % (v/v) MPD, 100 mM imidazole, pH = 7.0). Protein crystals were soaked in their respective precipitant solutions containing 50 mM BeCl2 and subsequently flash-frozen using 20% glycerol as cryoprotectant. Resolution 1.35 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 1–166; UniProt 1–166 Author chain B; 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 8cnj

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8cnj
Deposition date deposition_date2023-02-23
Structure title titleHRas(1-166) in complex with GDP and BeF3-
Keywords keywordssmall G protein, cellular signalling, metal fluorides, Ras superfamily, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.30
Radius of gyration Rg (electron density) rg_electron21.31
Forward intensity I(0) i028129500.00
Molecular weight molecular_weight38842.0 kDa
Excluded volume excluded_volume47761 ų
Envelope volume envelope_volume54878 ų
Hydration-shell volume shell_volume21926 ų
Envelope diameter envelope_diameter77.6
Shell Rg shell_rg27.67
Envelope Rg envelope_rg21.46
Shape Rg shape_rg21.33
Total Rg total_rg22.00
Total atoms total_atoms2718
Residues n_residues332
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 dmax76.9
Rg (real space) rg_real22.31
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real2.8130e+07
I(0) uncertainty (real space) i0_real_error4.0930e+05
Rg (reciprocal space) rg_reciprocal22.31
I(0) (reciprocal space) i0_reciprocal28130000.0000
Solution quality estimate total_estimate0.7893
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.6
Skewness Skewness skewness0.403
Kurtosis Kurtosis kurtosis-0.262
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4932000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.760; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)