9uwg

Structure of the human DCAF2-DDB1 complex

Method: ELECTRON MICROSCOPY Dmax: 96.5 Å Quality: EXCELLENT

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

DNA damage-binding protein 1

Homo sapiens

UniProt Q16531

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 1–1140 Not recorded Denticleless protein homolog × 1 (Q9NZJ0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.21 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.

202 other PDB entries and 290 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DDB1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 20–1159; UniProt 1–1140

Denticleless protein homolog

Homo sapiens

UniProt Q9NZJ0

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 B; UniProt 1–730 Not recorded DNA damage-binding protein 1 × 1 (Q16531) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.21 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 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DTL_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–730; UniProt 1–730

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 9uwg

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9uwg
Deposition date deposition_date2025-05-12
Structure title titleStructure of the human DCAF2-DDB1 complex
Keywords keywordsE3 ligase, ligase; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier31.92
Radius of gyration Rg (electron density) rg_electron30.79
Forward intensity I(0) i0241691000.00
Molecular weight molecular_weight125410.0 kDa
Excluded volume excluded_volume157450 ų
Envelope volume envelope_volume191430 ų
Hydration-shell volume shell_volume49616 ų
Envelope diameter envelope_diameter100.3
Shell Rg shell_rg39.53
Envelope Rg envelope_rg30.70
Shape Rg shape_rg30.78
Total Rg total_rg31.55
Total atoms total_atoms8822
Residues n_residues1123
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 dmax96.5
Rg (real space) rg_real31.69
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real2.4170e+08
I(0) uncertainty (real space) i0_real_error3.6960e+06
Rg (reciprocal space) rg_reciprocal31.80
I(0) (reciprocal space) i0_reciprocal241700000.0000
Solution quality estimate total_estimate0.9063
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.5
Skewness Skewness skewness0.096
Kurtosis Kurtosis kurtosis-0.580
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha50840000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.951; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.945

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)