9sa1

The RING domain of IDOL

Method: X-RAY DIFFRACTION Dmax: 59.1 Å Quality: REASONABLE

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

E3 ubiquitin-protein ligase MYLIP

Homo sapiens

UniProt Q8WY64

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 369–445 Chain B; UniProt 369–445 Not recorded ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;200 mM Magnesium chloride hexahydrate, 100 mM Bis-tris, 25% w/v PEG 3350 Resolution 1.06 Å R-free 0.177

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.

34 other PDB entries and 70 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYLIP_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–78; UniProt 369–445 Author chain B; PDBConstruct 2–78; UniProt 369–445

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 9sa1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9sa1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9sa1
Deposition date deposition_date2025-08-07
最后修订 last_revision2025-09-10
Structure title titleThe RING domain of IDOL
Keywords keywordsE3, ubiquitin, RING, Zinc finger, LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.40
Radius of gyration Rg (electron density) rg_electron16.38
Forward intensity I(0) i07079600.00
Molecular weight molecular_weight17863.0 kDa
Excluded volume excluded_volume21746 ų
Envelope volume envelope_volume25653 ų
Hydration-shell volume shell_volume13632 ų
Envelope diameter envelope_diameter58.0
Shell Rg shell_rg21.59
Envelope Rg envelope_rg16.78
Shape Rg shape_rg16.39
Total Rg total_rg17.25
Total atoms total_atoms1215
Residues n_residues156
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 dmax59.1
Rg (real space) rg_real17.37
Rg uncertainty (real space) rg_real_error0.41
I(0) (real space) i0_real7.0800e+06
I(0) uncertainty (real space) i0_real_error8.9350e+04
Rg (reciprocal space) rg_reciprocal17.37
I(0) (reciprocal space) i0_reciprocal7080000.0000
Solution quality estimate total_estimate0.7320
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary58.4
Skewness Skewness skewness0.300
Kurtosis Kurtosis kurtosis-0.300
Angular range angular_range— – 0.4550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha980000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.825; Stabil: 1.000; Sysdev: 0.363; Positv: 1.000; Valcen: 0.964; Smooth: 0.985

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)