10yh

DNA Ligase IIIa bound to a nucleosome containing a nick at SHL-6 (composite)

Method: ELECTRON MICROSCOPY Dmax: 140.2 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 3 PDB declaration: 12-meric(12) Consistent with all polymer counts Chain A; UniProt 39–135 Chain E; UniProt 39–135 Not recorded Histone H4 × 2 (P62805) Histone H2A type 1-H × 2 (Q96KK5) Histone H2B type 1-M × 2 (Q99879) 601 I strand (non-damaged strand) × 1 601 J strand (damaged strand 1) × 1 601 K strand (damaged strand 2) × 1 DNA ligase 3 × 1 (P49916) AMP ADENOSINE MONOPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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 1–97; UniProt 39–135 Author chain E; PDBConstruct 1–97; UniProt 39–135

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 3 PDB declaration: 12-meric(12) Consistent with all polymer counts Chain B; UniProt 23–102 Chain F; UniProt 23–102 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H2A type 1-H × 2 (Q96KK5) Histone H2B type 1-M × 2 (Q99879) 601 I strand (non-damaged strand) × 1 601 J strand (damaged strand 1) × 1 601 K strand (damaged strand 2) × 1 DNA ligase 3 × 1 (P49916) AMP ADENOSINE MONOPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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 1–80; UniProt 23–102 Author chain F; PDBConstruct 1–80; UniProt 23–102

Histone H2A type 1-H

Homo sapiens

UniProt Q96KK5

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 3 PDB declaration: 12-meric(12) Consistent with all polymer counts Chain C; UniProt 12–118 Chain G; UniProt 12–118 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2B type 1-M × 2 (Q99879) 601 I strand (non-damaged strand) × 1 601 J strand (damaged strand 1) × 1 601 K strand (damaged strand 2) × 1 DNA ligase 3 × 1 (P49916) AMP ADENOSINE MONOPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1H_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–107; UniProt 12–118 Author chain G; PDBConstruct 1–107; UniProt 12–118

Histone H2B type 1-M

Homo sapiens

UniProt Q99879

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 3 PDB declaration: 12-meric(12) Consistent with all polymer counts Chain D; UniProt 33–125 Chain H; UniProt 33–125 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2A type 1-H × 2 (Q96KK5) 601 I strand (non-damaged strand) × 1 601 J strand (damaged strand 1) × 1 601 K strand (damaged strand 2) × 1 DNA ligase 3 × 1 (P49916) AMP ADENOSINE MONOPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

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

View Construct and Data Evidence
UniProt name H2B1M_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–93; UniProt 33–125 Author chain H; PDBConstruct 1–93; UniProt 33–125

DNA ligase 3

Homo sapiens

UniProt P49916

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 3 PDB declaration: 12-meric(12) Consistent with all polymer counts Chain L; UniProt 474–681 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2A type 1-H × 2 (Q96KK5) Histone H2B type 1-M × 2 (Q99879) 601 I strand (non-damaged strand) × 1 601 J strand (damaged strand 1) × 1 601 K strand (damaged strand 2) × 1 AMP ADENOSINE MONOPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

12 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DNLI3_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain L; PDBConstruct 1–208; UniProt 474–681

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 10yh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 10yh
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2. Structure Basics 2. Structure Basics

Entry ID entry_id10yh
Deposition date deposition_date2026-02-12
Structure title titleDNA Ligase IIIa bound to a nucleosome containing a nick at SHL-6 (composite)
Keywords keywordsNucleosome, DNA Ligase IIIa, 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_guinier43.15
Radius of gyration Rg (electron density) rg_electron41.80
Forward intensity I(0) i0997126000.00
Molecular weight molecular_weight199350.0 kDa
Excluded volume excluded_volume224260 ų
Envelope volume envelope_volume340920 ų
Hydration-shell volume shell_volume68155 ų
Envelope diameter envelope_diameter142.7
Shell Rg shell_rg47.14
Envelope Rg envelope_rg41.25
Shape Rg shape_rg41.71
Total Rg total_rg42.23
Total atoms total_atoms13642
Residues n_residues1250
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 dmax140.2
Rg (real space) rg_real43.06
Rg uncertainty (real space) rg_real_error1.56
I(0) (real space) i0_real9.9710e+08
I(0) uncertainty (real space) i0_real_error1.8290e+07
Rg (reciprocal space) rg_reciprocal43.15
I(0) (reciprocal space) i0_reciprocal997200000.0000
Solution quality estimate total_estimate0.8820
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary45.5
Skewness Skewness skewness0.255
Kurtosis Kurtosis kurtosis-0.412
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha71180000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.891; Stabil: 0.995; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.810

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)