9bjz

Structure of the human DDD-Ube2e2 complex

Method: ELECTRON MICROSCOPY Dmax: 129.1 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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–395 Chain A; UniProt 706–1140 Mutation:residues 396-705 replaced with GNGNSG DET1 homolog × 1 (Q7L5Y6) DET1- and DDB1-associated protein 1 × 1 (Q9BW61) Ubiquitin-conjugating enzyme E2 E2 × 1 (Q96LR5) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.83 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 18–412; UniProt 1–395 Author chain A; PDBConstruct 419–853; UniProt 706–1140

DET1 homolog

Homo sapiens

UniProt Q7L5Y6

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 B; UniProt 2–550 Not recorded DNA damage-binding protein 1 × 1 (Q16531) DET1- and DDB1-associated protein 1 × 1 (Q9BW61) Ubiquitin-conjugating enzyme E2 E2 × 1 (Q96LR5) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.83 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.

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DET1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 41–589; UniProt 2–550

DET1- and DDB1-associated protein 1

Homo sapiens

UniProt Q9BW61

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 1–102 Not recorded DNA damage-binding protein 1 × 1 (Q16531) DET1 homolog × 1 (Q7L5Y6) Ubiquitin-conjugating enzyme E2 E2 × 1 (Q96LR5) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.83 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.

29 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DDA1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–102; UniProt 1–102

Ubiquitin-conjugating enzyme E2 E2

Homo sapiens

UniProt Q96LR5

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 D; UniProt 2–201 Not recorded DNA damage-binding protein 1 × 1 (Q16531) DET1 homolog × 1 (Q7L5Y6) DET1- and DDB1-associated protein 1 × 1 (Q9BW61) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.83 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.

9 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UB2E2_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 21–220; UniProt 2–201

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 9bjz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9bjz
Deposition date deposition_date2024-04-26
Structure title titleStructure of the human DDD-Ube2e2 complex
Keywords keywordsDDB1, DDA1, DET1, DCAF, ubiquitin conjugating enzyme, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier38.53
Radius of gyration Rg (electron density) rg_electron38.01
Forward intensity I(0) i0433790000.00
Molecular weight molecular_weight170300.0 kDa
Excluded volume excluded_volume213470 ų
Envelope volume envelope_volume281100 ų
Hydration-shell volume shell_volume61100 ų
Envelope diameter envelope_diameter136.4
Shell Rg shell_rg44.36
Envelope Rg envelope_rg37.88
Shape Rg shape_rg37.99
Total Rg total_rg38.45
Total atoms total_atoms23649
Residues n_residues1527
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 dmax129.1
Rg (real space) rg_real38.55
Rg uncertainty (real space) rg_real_error0.92
I(0) (real space) i0_real4.3380e+08
I(0) uncertainty (real space) i0_real_error6.7270e+06
Rg (reciprocal space) rg_reciprocal38.54
I(0) (reciprocal space) i0_reciprocal433800000.0000
Solution quality estimate total_estimate0.8714
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.1
Skewness Skewness skewness0.407
Kurtosis Kurtosis kurtosis-0.182
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha115100000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.833; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.824

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)