9sdy

Structure of RBR E2 variant binding to CUL5-RBX2 bound ARIH2

Method: ELECTRON MICROSCOPY Dmax: 147.7 Å Quality: GOOD

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

RING-box protein 2

Homo sapiens

UniProt Q9UBF6

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain R; UniProt 1–113 Not recorded L3A2-1 × 1 Cullin-5 × 1 (Q93034) E3 ubiquitin-protein ligase ARIH2 × 1 (O95376) ZN ZINC ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.06 Å

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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBX2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain R; PDBConstruct 1–113; UniProt 1–113

Cullin-5

Homo sapiens

UniProt Q93034

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–780 Not recorded L3A2-1 × 1 RING-box protein 2 × 1 (Q9UBF6) E3 ubiquitin-protein ligase ARIH2 × 1 (O95376) ZN ZINC ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.06 Å

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.

13 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CUL5_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–780; UniProt 1–780

E3 ubiquitin-protein ligase ARIH2

Homo sapiens

UniProt O95376

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain H; UniProt 1–493 Not recorded L3A2-1 × 1 RING-box protein 2 × 1 (Q9UBF6) Cullin-5 × 1 (Q93034) ZN ZINC ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.06 Å

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.

4 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARI2_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain H; PDBConstruct 1–493; UniProt 1–493

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 9sdy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9sdy
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9sdy
Deposition date deposition_date2025-08-15
Structure title titleStructure of RBR E2 variant binding to CUL5-RBX2 bound ARIH2
Keywords keywordsComplex, Ligase; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier45.12
Radius of gyration Rg (electron density) rg_electron45.32
Forward intensity I(0) i0256329000.00
Molecular weight molecular_weight129420.0 kDa
Excluded volume excluded_volume161350 ų
Envelope volume envelope_volume254650 ų
Hydration-shell volume shell_volume49658 ų
Envelope diameter envelope_diameter152.7
Shell Rg shell_rg46.15
Envelope Rg envelope_rg44.54
Shape Rg shape_rg45.37
Total Rg total_rg45.21
Total atoms total_atoms9073
Residues n_residues1172
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 dmax147.7
Rg (real space) rg_real45.16
Rg uncertainty (real space) rg_real_error1.30
I(0) (real space) i0_real2.5630e+08
I(0) uncertainty (real space) i0_real_error4.4250e+06
Rg (reciprocal space) rg_reciprocal45.12
I(0) (reciprocal space) i0_reciprocal256300000.0000
Solution quality estimate total_estimate0.8960
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary50.6
Skewness Skewness skewness0.211
Kurtosis Kurtosis kurtosis-0.708
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14160000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.949; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.943; Smooth: 0.855

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)