9lu1

protein structure of DDB1-DDA1-DET1-Ube2e2 bound to COP1 dimer

Method: ELECTRON MICROSCOPY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

E3 ubiquitin-protein ligase COP1

Homo sapiens

UniProt Q8NHY2

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 6 DET1- and DDB1-associated protein 1 × 1 (Q9BW61) Ubiquitin-conjugating enzyme E2 E2 × 1 (Q96LR5) DET1 homolog × 1 (Q7L5Y6) DNA damage-binding protein 1 × 1 (Q16531) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name COP1_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–731; UniProt 1–731 Author chain E; PDBConstruct 1–731; UniProt 1–731

DET1- and DDB1-associated protein 1

Homo sapiens

UniProt Q9BW61

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 6 E3 ubiquitin-protein ligase COP1 × 2 (Q8NHY2) Ubiquitin-conjugating enzyme E2 E2 × 1 (Q96LR5) DET1 homolog × 1 (Q7L5Y6) DNA damage-binding protein 1 × 1 (Q16531) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name DDA1_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–102; UniProt 1–102

Ubiquitin-conjugating enzyme E2 E2

Homo sapiens

UniProt Q96LR5

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 6 E3 ubiquitin-protein ligase COP1 × 2 (Q8NHY2) DET1- and DDB1-associated protein 1 × 1 (Q9BW61) DET1 homolog × 1 (Q7L5Y6) DNA damage-binding protein 1 × 1 (Q16531) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name UB2E2_HUMAN
Isoform —
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–201; UniProt 1–201

DET1 homolog

Homo sapiens

UniProt Q7L5Y6

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 6 E3 ubiquitin-protein ligase COP1 × 2 (Q8NHY2) DET1- and DDB1-associated protein 1 × 1 (Q9BW61) Ubiquitin-conjugating enzyme E2 E2 × 1 (Q96LR5) DNA damage-binding protein 1 × 1 (Q16531) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name DET1_HUMAN
Isoform —
PDB entities 4
Chains and sequence ranges Author chain R; PDBConstruct 1–550; UniProt 1–550

DNA damage-binding protein 1

Homo sapiens

UniProt Q16531

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 6 E3 ubiquitin-protein ligase COP1 × 2 (Q8NHY2) DET1- and DDB1-associated protein 1 × 1 (Q9BW61) Ubiquitin-conjugating enzyme E2 E2 × 1 (Q96LR5) DET1 homolog × 1 (Q7L5Y6) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name DDB1_HUMAN
Isoform —
PDB entities 5
Chains and sequence ranges Author chain S; PDBConstruct 1–1140; 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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id9lu1
Deposition date deposition_date2025-02-07
Structure title titleprotein structure of DDB1-DDA1-DET1-Ube2e2 bound to COP1 dimer
Keywords keywordsE3 ligase, LIGASE; LIGASE
Experimental Method methodELECTRON MICROSCOPY
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

9lu1__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

9lu1__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

9lu1__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)50.79 Å
Rg (electron density)49.60 Å
Total Rg49.17 Å
Atom count17116
Residues2589
Excluded volume298170 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 9lu1__assembly_1__model_1 hexameric (6) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (5)

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7. Citations (1)