8vwv

OGG1 bound to a nucleosome containing 8oxoG at SHL4 (composite map)

Method: ELECTRON MICROSCOPY Dmax: 147.1 Å Quality: GOOD

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

Histone H3.2

Homo sapiens

UniProt Q71DI3

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–DNA Heteromer Protein × 9 DNA 2 PDB declaration: 11-meric(11) Consistent with all polymer counts Chain A; UniProt 2–136 Chain E; UniProt 2–136 Not recorded Histone H4 × 2 (P62805) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-C/E/F/G/I × 2 (P62807) 601 I strand (damaged strand) × 1 601 J strand (non-damaged) × 1 N-glycosylase/DNA lyase × 1 (O15527) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.1;50 mM HEPES (pH-7.1), 100 mM NaCl, 1 mM TCEP, and 1 mM EDTA cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

139 other PDB entries and 157 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H32_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–135; UniProt 2–136 Author chain E; PDBConstruct 1–135; UniProt 2–136

Histone H4

Homo sapiens

UniProt P62805

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–DNA Heteromer Protein × 9 DNA 2 PDB declaration: 11-meric(11) Consistent with all polymer counts Chain B; UniProt 2–103 Chain F; UniProt 2–103 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-C/E/F/G/I × 2 (P62807) 601 I strand (damaged strand) × 1 601 J strand (non-damaged) × 1 N-glycosylase/DNA lyase × 1 (O15527) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.1;50 mM HEPES (pH-7.1), 100 mM NaCl, 1 mM TCEP, and 1 mM EDTA cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

581 other PDB entries and 633 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–102; UniProt 2–103 Author chain F; PDBConstruct 1–102; UniProt 2–103

Histone H2A type 1

Homo sapiens

UniProt P0C0S8

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–DNA Heteromer Protein × 9 DNA 2 PDB declaration: 11-meric(11) Consistent with all polymer counts Chain C; UniProt 2–130 Chain G; UniProt 2–130 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2B type 1-C/E/F/G/I × 2 (P62807) 601 I strand (damaged strand) × 1 601 J strand (non-damaged) × 1 N-glycosylase/DNA lyase × 1 (O15527) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.1;50 mM HEPES (pH-7.1), 100 mM NaCl, 1 mM TCEP, and 1 mM EDTA cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

49 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–129; UniProt 2–130 Author chain G; PDBConstruct 1–129; UniProt 2–130

Histone H2B type 1-C/E/F/G/I

Homo sapiens

UniProt P62807

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–DNA Heteromer Protein × 9 DNA 2 PDB declaration: 11-meric(11) Consistent with all polymer counts Chain D; UniProt 2–126 Chain H; UniProt 2–126 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2A type 1 × 2 (P0C0S8) 601 I strand (damaged strand) × 1 601 J strand (non-damaged) × 1 N-glycosylase/DNA lyase × 1 (O15527) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.1;50 mM HEPES (pH-7.1), 100 mM NaCl, 1 mM TCEP, and 1 mM EDTA cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

79 other PDB entries and 79 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1C_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–125; UniProt 2–126 Author chain H; PDBConstruct 1–125; UniProt 2–126

N-glycosylase/DNA lyase

Homo sapiens

UniProt O15527

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–DNA Heteromer Protein × 9 DNA 2 PDB declaration: 11-meric(11) Consistent with all polymer counts Chain K; UniProt 1–345 Mutation:Q249K Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-C/E/F/G/I × 2 (P62807) 601 I strand (damaged strand) × 1 601 J strand (non-damaged) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.1;50 mM HEPES (pH-7.1), 100 mM NaCl, 1 mM TCEP, and 1 mM EDTA cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

46 other PDB entries and 54 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name OGG1_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain K; PDBConstruct 1–345; UniProt 1–345

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 8vwv

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8vwv
Deposition date deposition_date2024-02-02
Structure title titleOGG1 bound to a nucleosome containing 8oxoG at SHL4 (composite map)
Keywords keywordsNucleosome, 8-oxo-guanine DNA Glycosylase I, DNA Repair, DNA BINDING PROTEIN, DNA BINDING PROTEIN-DNA complex; DNA BINDING PROTEIN/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.05
Radius of gyration Rg (electron density) rg_electron42.87
Forward intensity I(0) i01092120000.00
Molecular weight molecular_weight210970.0 kDa
Excluded volume excluded_volume238560 ų
Envelope volume envelope_volume361570 ų
Hydration-shell volume shell_volume71110 ų
Envelope diameter envelope_diameter157.4
Shell Rg shell_rg47.38
Envelope Rg envelope_rg42.25
Shape Rg shape_rg42.81
Total Rg total_rg43.19
Total atoms total_atoms14474
Residues n_residues1359
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 dmax147.1
Rg (real space) rg_real43.96
Rg uncertainty (real space) rg_real_error1.42
I(0) (real space) i0_real1.0920e+09
I(0) uncertainty (real space) i0_real_error2.1050e+07
Rg (reciprocal space) rg_reciprocal44.05
I(0) (reciprocal space) i0_reciprocal1092000000.0000
Solution quality estimate total_estimate0.8821
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.269
Kurtosis Kurtosis kurtosis-0.349
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha88700000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.860; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.883

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)