8wwc

De novo design binder of HRAS -120-4

Method: X-RAY DIFFRACTION Dmax: 105.2 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 De novo design protein 120-4 × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;0.1M Bis Tris Propane pH7.5 0.2M Sodium nitrate 20% w/v PEG3350 10%v/v Ethylene glycol Resolution 2.80 Å R-free 0.247
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–166 Not recorded De novo design protein 120-4 × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;0.1M Bis Tris Propane pH7.5 0.2M Sodium nitrate 20% w/v PEG3350 10%v/v Ethylene glycol Resolution 2.80 Å R-free 0.247

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 2
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 8wwc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8wwc
Deposition date deposition_date2023-10-25
Structure title titleDe novo design binder of HRAS -120-4
Keywords keywordsDe novo design protein, DE NOVO PROTEIN; DE NOVO PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.96
Radius of gyration Rg (electron density) rg_electron28.77
Forward intensity I(0) i059856900.00
Molecular weight molecular_weight57932.0 kDa
Excluded volume excluded_volume71224 ų
Envelope volume envelope_volume90928 ų
Hydration-shell volume shell_volume28090 ų
Envelope diameter envelope_diameter110.5
Shell Rg shell_rg33.42
Envelope Rg envelope_rg29.79
Shape Rg shape_rg28.79
Total Rg total_rg29.15
Total atoms total_atoms4060
Residues n_residues553
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 dmax105.2
Rg (real space) rg_real29.31
Rg uncertainty (real space) rg_real_error1.05
I(0) (real space) i0_real5.9860e+07
I(0) uncertainty (real space) i0_real_error9.3890e+05
Rg (reciprocal space) rg_reciprocal29.16
I(0) (reciprocal space) i0_reciprocal59850000.0000
Solution quality estimate total_estimate0.7718
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.8
Skewness Skewness skewness0.714
Kurtosis Kurtosis kurtosis0.153
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13770000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.567; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.541; Smooth: 0.789

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)