9pvh

Human Cullin-4 in complex with CAND2

Method: ELECTRON MICROSCOPY Dmax: 157.6 Å Quality: REASONABLE

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

Cullin-4A

Homo sapiens

UniProt Q13619

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 37–759 Not recorded Cullin-associated NEDD8-dissociated protein 2 × 1 (O75155) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 4.38 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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CUL4A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–726; UniProt 37–759

Cullin-associated NEDD8-dissociated protein 2

Homo sapiens

UniProt O75155

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 C; UniProt 1–1236 Not recorded Cullin-4A × 1 (Q13619) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 4.38 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CAND2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 12–1247; UniProt 1–1236

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 9pvh

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9pvh
Deposition date deposition_date2025-08-01
Structure title titleHuman Cullin-4 in complex with CAND2
Keywords keywordsComplex, LIGASE; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.70
Radius of gyration Rg (electron density) rg_electron47.44
Forward intensity I(0) i0615945000.00
Molecular weight molecular_weight207680.0 kDa
Excluded volume excluded_volume261780 ų
Envelope volume envelope_volume415510 ų
Hydration-shell volume shell_volume74150 ų
Envelope diameter envelope_diameter160.9
Shell Rg shell_rg51.36
Envelope Rg envelope_rg45.65
Shape Rg shape_rg47.45
Total Rg total_rg47.58
Total atoms total_atoms14580
Residues n_residues1862
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 dmax157.6
Rg (real space) rg_real49.27
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real6.1330e+08
I(0) uncertainty (real space) i0_real_error9.8050e+06
Rg (reciprocal space) rg_reciprocal47.70
I(0) (reciprocal space) i0_reciprocal616000000.0000
Solution quality estimate total_estimate0.6959
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.5
Skewness Skewness skewness0.397
Kurtosis Kurtosis kurtosis-0.277
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha1.4740
Highest regularization parameter α highest_alpha53910000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.937; Stabil: 0.899; Sysdev: 0.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.584

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)