8zsw

Crystal Structure of Human DDB1, a Component of the E3 Ubiquitin Ligase Complex

Method: X-RAY DIFFRACTION Dmax: 117.4 Å Quality: GOOD

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–1140 Not recorded ACT ACETATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;287 K;0.1M MES (pH 6.5), 0.1M sodium acetate, 27%(w/v) PEG 400 Resolution 2.25 Å R-free 0.229

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

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 8zsw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8zsw
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8zsw
Deposition date deposition_date2024-06-05
最后修订 last_revision2025-06-11
Structure title titleCrystal Structure of Human DDB1, a Component of the E3 Ubiquitin Ligase Complex
Keywords keywordsE3 ubiquitin ligase component, DDB1, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier35.53
Radius of gyration Rg (electron density) rg_electron34.85
Forward intensity I(0) i0232219000.00
Molecular weight molecular_weight123730.0 kDa
Excluded volume excluded_volume155360 ų
Envelope volume envelope_volume202040 ų
Hydration-shell volume shell_volume48359 ų
Envelope diameter envelope_diameter121.3
Shell Rg shell_rg41.29
Envelope Rg envelope_rg34.52
Shape Rg shape_rg34.85
Total Rg total_rg35.30
Total atoms total_atoms8695
Residues n_residues1110
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 dmax117.4
Rg (real space) rg_real35.49
Rg uncertainty (real space) rg_real_error1.02
I(0) (real space) i0_real2.3220e+08
I(0) uncertainty (real space) i0_real_error4.3800e+06
Rg (reciprocal space) rg_reciprocal35.52
I(0) (reciprocal space) i0_reciprocal232200000.0000
Solution quality estimate total_estimate0.8929
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.1
Skewness Skewness skewness0.283
Kurtosis Kurtosis kurtosis-0.445
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha37320000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.892; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.928

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)