9y0i

Crystal structure of designed switching homodimer CSD20f3A

Method: X-RAY DIFFRACTION Dmax: 79.0 Å Quality: EXCELLENT

1. Protein Identity and Related Structures Protein Identity & Related Structures

No usable UniProt protein identity is available for this entry.

七张关系表仍保留该条目的 assembly 与组成信息,但缺少统一蛋白身份时,不能可靠建立跨 PDB 的同蛋白Chain接。

Assembly Composition of the Current Entry

Assembly Oligomeric State 实体与Construct证据 Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein homooligomer Homooligomer 蛋白 2 / DNA 0 / RNA 0 / 其他Polymer 0 PDB declaration: dimeric Entity 1:CSD20f3A × 2 缺少 UniProt 身份时不显示参考序列区间 Not recorded No recorded non-water small molecule X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;0.2 M Ammonium acetate, 0.1 M BIS-Tris pH 5.5 and 25 % w/v PEG 3350 Resolution 2.66 Å R-free 0.282
2 Protein homooligomer Homooligomer 蛋白 2 / DNA 0 / RNA 0 / 其他Polymer 0 PDB declaration: dimeric Entity 1:CSD20f3A × 2 缺少 UniProt 身份时不显示参考序列区间 Not recorded No recorded non-water small molecule X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;0.2 M Ammonium acetate, 0.1 M BIS-Tris pH 5.5 and 25 % w/v PEG 3350 Resolution 2.66 Å R-free 0.282

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 9y0i

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9y0i
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9y0i
Deposition date deposition_date2025-08-28
最后修订 last_revision2025-09-10
Structure title titleCrystal structure of designed switching homodimer CSD20f3A
Keywords keywordsde novo protein, design model, Effector, kinetics and dynamics, Protein-protein interactions; DE NOVO PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.87
Radius of gyration Rg (electron density) rg_electron24.68
Forward intensity I(0) i088107600.00
Molecular weight molecular_weight69886.0 kDa
Excluded volume excluded_volume86508 ų
Envelope volume envelope_volume105380 ų
Hydration-shell volume shell_volume34204 ų
Envelope diameter envelope_diameter81.3
Shell Rg shell_rg33.11
Envelope Rg envelope_rg24.78
Shape Rg shape_rg24.67
Total Rg total_rg25.57
Total atoms total_atoms4910
Residues n_residues655
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 dmax79.0
Rg (real space) rg_real25.73
Rg uncertainty (real space) rg_real_error0.41
I(0) (real space) i0_real8.8110e+07
I(0) uncertainty (real space) i0_real_error1.2200e+06
Rg (reciprocal space) rg_reciprocal25.78
I(0) (reciprocal space) i0_reciprocal88110000.0000
Solution quality estimate total_estimate0.9038
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary77.7
Skewness Skewness skewness0.190
Kurtosis Kurtosis kurtosis-0.450
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha20840000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.927; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.981

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)