9kqo

cryo-EM structure of RNF20/RNF40-RAD6A-Ub in complex with H2BS112GlcNAc nucleosome

Method: ELECTRON MICROSCOPY Dmax: 121.4 Å Quality: GOOD

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

E3 ubiquitin-protein ligase BRE1B

Homo sapiens

UniProt O75150

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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain A; UniProt 941–1000 Not recorded Polyubiquitin-B × 1 (J3QS39) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-K × 2 (O60814) Histone H3 × 2 (A0A653DHJ5) Histone H4 × 2 (P62805) DNA (147-MER) × 1 DNA (147-MER) × 1 E3 ubiquitin-protein ligase BRE1A × 1 (Q5VTR2) Ubiquitin-conjugating enzyme E2 A × 1 (P49459) ZN ZINC ION × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.48 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BRE1B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–60; UniProt 941–1000

Polyubiquitin-B

Homo sapiens

UniProt J3QS39

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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain B; UniProt 1–75 Not recorded E3 ubiquitin-protein ligase BRE1B × 1 (O75150) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-K × 2 (O60814) Histone H3 × 2 (A0A653DHJ5) Histone H4 × 2 (P62805) DNA (147-MER) × 1 DNA (147-MER) × 1 E3 ubiquitin-protein ligase BRE1A × 1 (Q5VTR2) Ubiquitin-conjugating enzyme E2 A × 1 (P49459) ZN ZINC ION × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.48 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.

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

View Construct and Data Evidence
UniProt name J3QS39_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–75; UniProt 1–75

Histone H2A type 1-B/E

Homo sapiens

UniProt P04908

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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain C; UniProt 2–130 Chain G; UniProt 2–130 Not recorded E3 ubiquitin-protein ligase BRE1B × 1 (O75150) Polyubiquitin-B × 1 (J3QS39) Histone H2B type 1-K × 2 (O60814) Histone H3 × 2 (A0A653DHJ5) Histone H4 × 2 (P62805) DNA (147-MER) × 1 DNA (147-MER) × 1 E3 ubiquitin-protein ligase BRE1A × 1 (Q5VTR2) Ubiquitin-conjugating enzyme E2 A × 1 (P49459) ZN ZINC ION × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.48 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.

343 other PDB entries and 350 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1B_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-K

Homo sapiens

UniProt O60814

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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain D; UniProt 2–126 Chain H; UniProt 2–126 Not recorded E3 ubiquitin-protein ligase BRE1B × 1 (O75150) Polyubiquitin-B × 1 (J3QS39) Histone H2A type 1-B/E × 2 (P04908) Histone H3 × 2 (A0A653DHJ5) Histone H4 × 2 (P62805) DNA (147-MER) × 1 DNA (147-MER) × 1 E3 ubiquitin-protein ligase BRE1A × 1 (Q5VTR2) Ubiquitin-conjugating enzyme E2 A × 1 (P49459) ZN ZINC ION × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.48 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.

82 other PDB entries and 82 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1K_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

Histone H3

Homo sapiens

UniProt A0A653DHJ5

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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain E; UniProt 2–136 Chain K; UniProt 2–136 Not recorded E3 ubiquitin-protein ligase BRE1B × 1 (O75150) Polyubiquitin-B × 1 (J3QS39) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-K × 2 (O60814) Histone H4 × 2 (P62805) DNA (147-MER) × 1 DNA (147-MER) × 1 E3 ubiquitin-protein ligase BRE1A × 1 (Q5VTR2) Ubiquitin-conjugating enzyme E2 A × 1 (P49459) ZN ZINC ION × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.48 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A653DHJ5_CALMS
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–135; UniProt 2–136 Author chain K; 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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain F; UniProt 2–103 Chain L; UniProt 2–103 Not recorded E3 ubiquitin-protein ligase BRE1B × 1 (O75150) Polyubiquitin-B × 1 (J3QS39) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-K × 2 (O60814) Histone H3 × 2 (A0A653DHJ5) DNA (147-MER) × 1 DNA (147-MER) × 1 E3 ubiquitin-protein ligase BRE1A × 1 (Q5VTR2) Ubiquitin-conjugating enzyme E2 A × 1 (P49459) ZN ZINC ION × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.48 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 6
Chains and sequence ranges Author chain F; PDBConstruct 1–102; UniProt 2–103 Author chain L; PDBConstruct 1–102; UniProt 2–103

E3 ubiquitin-protein ligase BRE1A

Homo sapiens

UniProt Q5VTR2

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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain M; UniProt 915–974 Not recorded E3 ubiquitin-protein ligase BRE1B × 1 (O75150) Polyubiquitin-B × 1 (J3QS39) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-K × 2 (O60814) Histone H3 × 2 (A0A653DHJ5) Histone H4 × 2 (P62805) DNA (147-MER) × 1 DNA (147-MER) × 1 Ubiquitin-conjugating enzyme E2 A × 1 (P49459) ZN ZINC ION × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.48 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BRE1A_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain M; PDBConstruct 1–60; UniProt 915–974

Ubiquitin-conjugating enzyme E2 A

Homo sapiens

UniProt P49459

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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain R; UniProt 1–150 Not recorded E3 ubiquitin-protein ligase BRE1B × 1 (O75150) Polyubiquitin-B × 1 (J3QS39) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-K × 2 (O60814) Histone H3 × 2 (A0A653DHJ5) Histone H4 × 2 (P62805) DNA (147-MER) × 1 DNA (147-MER) × 1 E3 ubiquitin-protein ligase BRE1A × 1 (Q5VTR2) ZN ZINC ION × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.48 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBE2A_HUMAN
Isoform
PDB entities 10
Chains and sequence ranges Author chain R; PDBConstruct 1–150; UniProt 1–150

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 9kqo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9kqo
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9kqo
Deposition date deposition_date2024-11-26
Structure title titlecryo-EM structure of RNF20/RNF40-RAD6A-Ub in complex with H2BS112GlcNAc nucleosome
Keywords keywordsRNF20, RNF40, H2BS112GlcNAc, O-GlcNAcylation, ubiquitination, H2BK120Ub, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier42.10
Radius of gyration Rg (electron density) rg_electron39.91
Forward intensity I(0) i01133310000.00
Molecular weight molecular_weight214440.0 kDa
Excluded volume excluded_volume242370 ų
Envelope volume envelope_volume369020 ų
Hydration-shell volume shell_volume74259 ų
Envelope diameter envelope_diameter126.5
Shell Rg shell_rg47.95
Envelope Rg envelope_rg39.00
Shape Rg shape_rg39.79
Total Rg total_rg40.53
Total atoms total_atoms14687
Residues n_residues1399
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 dmax121.4
Rg (real space) rg_real41.81
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real1.1330e+09
I(0) uncertainty (real space) i0_real_error1.7620e+07
Rg (reciprocal space) rg_reciprocal42.09
I(0) (reciprocal space) i0_reciprocal1134000000.0000
Solution quality estimate total_estimate0.8971
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary54.3
Skewness Skewness skewness-0.007
Kurtosis Kurtosis kurtosis-0.643
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha80730000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.975; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.751

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

8. Citations (1)

9. Files and Curves (10)