8qh5

CryoEM structure of UVSSA(VHS)-CSA-DDB1-DDA1

Method: ELECTRON MICROSCOPY Dmax: 143.1 Å Quality: GOOD

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

UV-stimulated scaffold protein A

Homo sapiens

UniProt Q2YD98

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 1–709 Not recorded DNA excision repair protein ERCC-8 × 1 (Q13216) DNA damage-binding protein 1 × 1 (Q16531) DET1- and DDB1-associated protein 1 × 1 (Q9BW61) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 UVSSA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain D; PDBConstruct 21–729; UniProt 1–709

DNA excision repair protein ERCC-8

Homo sapiens

UniProt Q13216

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 1–396 Not recorded UV-stimulated scaffold protein A × 1 (Q2YD98) DNA damage-binding protein 1 × 1 (Q16531) DET1- and DDB1-associated protein 1 × 1 (Q9BW61) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ERCC8_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–396; UniProt 1–396

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 B; UniProt 1–1140 Not recorded UV-stimulated scaffold protein A × 1 (Q2YD98) DNA excision repair protein ERCC-8 × 1 (Q13216) DET1- and DDB1-associated protein 1 × 1 (Q9BW61) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 3
Chains and sequence ranges Author chain B; PDBConstruct 21–1160; UniProt 1–1140

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–102 Not recorded UV-stimulated scaffold protein A × 1 (Q2YD98) DNA excision repair protein ERCC-8 × 1 (Q13216) DNA damage-binding protein 1 × 1 (Q16531) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 4
Chains and sequence ranges Author chain C; 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 8qh5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8qh5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8qh5
Deposition date deposition_date2023-09-06
Structure title titleCryoEM structure of UVSSA(VHS)-CSA-DDB1-DDA1
Keywords keywordsUbiquitin ligase, DNA repair, LIGASE; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.28
Radius of gyration Rg (electron density) rg_electron40.98
Forward intensity I(0) i0539275000.00
Molecular weight molecular_weight189330.0 kDa
Excluded volume excluded_volume236900 ų
Envelope volume envelope_volume311520 ų
Hydration-shell volume shell_volume64723 ų
Envelope diameter envelope_diameter152.6
Shell Rg shell_rg45.02
Envelope Rg envelope_rg40.99
Shape Rg shape_rg40.96
Total Rg total_rg41.24
Total atoms total_atoms22744
Residues n_residues1687
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 dmax143.1
Rg (real space) rg_real41.40
Rg uncertainty (real space) rg_real_error1.38
I(0) (real space) i0_real5.3930e+08
I(0) uncertainty (real space) i0_real_error1.0700e+07
Rg (reciprocal space) rg_reciprocal41.28
I(0) (reciprocal space) i0_reciprocal539200000.0000
Solution quality estimate total_estimate0.8500
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary49.0
Skewness Skewness skewness0.522
Kurtosis Kurtosis kurtosis0.029
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha108000000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.746; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.808

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)