8roy

Structure of the human DDB1-DDA1-DCAF15 E3 ubiquitin ligase bound to compound furan 24

Method: ELECTRON MICROSCOPY Dmax: 103.6 Å Quality: EXCELLENT

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

DDB1- and CUL4-associated factor 15

Homo sapiens

UniProt Q66K64

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–600 Not recorded DNA damage-binding protein 1 × 1 (Q16531) DET1- and DDB1-associated protein 1 × 1 (Q9BW61) A1H18 1-[5-[[3,4-bis(chloranyl)-1~{H}-indol-7-yl]sulfamoyl]-3-methyl-furan-2-yl]carbonyl-~{N}-methyl-piperidine-4-carboxamide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DCA15_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–603; UniProt 1–600

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–395 Chain B; UniProt 706–1140 Not recorded DDB1- and CUL4-associated factor 15 × 1 (Q66K64) DET1- and DDB1-associated protein 1 × 1 (Q9BW61) A1H18 1-[5-[[3,4-bis(chloranyl)-1~{H}-indol-7-yl]sulfamoyl]-3-methyl-furan-2-yl]carbonyl-~{N}-methyl-piperidine-4-carboxamide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–395; UniProt 1–395 Author chain B; PDBConstruct 402–836; UniProt 706–1140

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 1–102 Not recorded DDB1- and CUL4-associated factor 15 × 1 (Q66K64) DNA damage-binding protein 1 × 1 (Q16531) A1H18 1-[5-[[3,4-bis(chloranyl)-1~{H}-indol-7-yl]sulfamoyl]-3-methyl-furan-2-yl]carbonyl-~{N}-methyl-piperidine-4-carboxamide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 D; PDBConstruct 1–102; UniProt 1–102

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 8roy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8roy
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8roy
Deposition date deposition_date2024-01-12
Structure title titleStructure of the human DDB1-DDA1-DCAF15 E3 ubiquitin ligase bound to compound furan 24
Keywords keywordsE3 ligase, Complex, LIGASE; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier33.40
Radius of gyration Rg (electron density) rg_electron32.47
Forward intensity I(0) i0210713000.00
Molecular weight molecular_weight117240.0 kDa
Excluded volume excluded_volume147100 ų
Envelope volume envelope_volume199520 ų
Hydration-shell volume shell_volume49788 ų
Envelope diameter envelope_diameter112.9
Shell Rg shell_rg40.38
Envelope Rg envelope_rg32.28
Shape Rg shape_rg32.50
Total Rg total_rg33.04
Total atoms total_atoms8294
Residues n_residues1174
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 dmax103.6
Rg (real space) rg_real33.26
Rg uncertainty (real space) rg_real_error0.52
I(0) (real space) i0_real2.1070e+08
I(0) uncertainty (real space) i0_real_error2.9540e+06
Rg (reciprocal space) rg_reciprocal33.35
I(0) (reciprocal space) i0_reciprocal210700000.0000
Solution quality estimate total_estimate0.9033
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.9
Skewness Skewness skewness0.167
Kurtosis Kurtosis kurtosis-0.477
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha49880000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.936; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.936

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)