8ieg

Bre1(mRBD-RING)/Rad6-Ub/nucleosome complex

Method: ELECTRON MICROSCOPY Dmax: 119.7 Å Quality: GOOD

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

Histone H3.1

Homo sapiens

UniProt P68431

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 × 11 DNA 2 PDB declaration: tridecameric(13) Consistent with all polymer counts Chain E; UniProt 38–135 Chain K; UniProt 38–135 Not recorded Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-K × 1 (O60814) Histone H2B type 1-K × 1 (O60814) DNA (147-MER) × 1 DNA (147-MER) × 1 E3 ubiquitin-protein ligase BRE1 × 2 (Q07457) Ubiquitin-conjugating enzyme E2 2 × 1 (P06104) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.44 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.

402 other PDB entries and 475 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H31_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain E; PDBConstruct 1–98; UniProt 38–135 Author chain K; PDBConstruct 1–98; UniProt 38–135

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 × 11 DNA 2 PDB declaration: tridecameric(13) Consistent with all polymer counts Chain F; UniProt 23–102 Chain L; UniProt 23–102 Not recorded Histone H3.1 × 2 (P68431) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-K × 1 (O60814) Histone H2B type 1-K × 1 (O60814) DNA (147-MER) × 1 DNA (147-MER) × 1 E3 ubiquitin-protein ligase BRE1 × 2 (Q07457) Ubiquitin-conjugating enzyme E2 2 × 1 (P06104) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.44 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 F; PDBConstruct 1–80; UniProt 23–102 Author chain L; PDBConstruct 1–80; UniProt 23–102

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 × 11 DNA 2 PDB declaration: tridecameric(13) Consistent with all polymer counts Chain C; UniProt 11–119 Chain G; UniProt 11–119 Not recorded Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2B type 1-K × 1 (O60814) Histone H2B type 1-K × 1 (O60814) DNA (147-MER) × 1 DNA (147-MER) × 1 E3 ubiquitin-protein ligase BRE1 × 2 (Q07457) Ubiquitin-conjugating enzyme E2 2 × 1 (P06104) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.44 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 1–109; UniProt 11–119 Author chain G; PDBConstruct 1–109; UniProt 11–119

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 × 11 DNA 2 PDB declaration: tridecameric(13) Consistent with all polymer counts Chain D; UniProt 32–125 Chain H; UniProt 32–125 Not recorded Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) DNA (147-MER) × 1 DNA (147-MER) × 1 E3 ubiquitin-protein ligase BRE1 × 2 (Q07457) Ubiquitin-conjugating enzyme E2 2 × 1 (P06104) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.44 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, 5
Chains and sequence ranges Author chain D; PDBConstruct 1–94; UniProt 32–125 Author chain H; PDBConstruct 1–94; UniProt 32–125

E3 ubiquitin-protein ligase BRE1

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt Q07457

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 × 11 DNA 2 PDB declaration: tridecameric(13) Consistent with all polymer counts Chain A; UniProt 637–700 Chain B; UniProt 637–700 Not recorded Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-K × 1 (O60814) Histone H2B type 1-K × 1 (O60814) DNA (147-MER) × 1 DNA (147-MER) × 1 Ubiquitin-conjugating enzyme E2 2 × 1 (P06104) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.44 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BRE1_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain A; PDBConstruct 1–64; UniProt 637–700 Author chain B; PDBConstruct 1–64; UniProt 637–700

Ubiquitin-conjugating enzyme E2 2

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P06104

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 × 11 DNA 2 PDB declaration: tridecameric(13) Consistent with all polymer counts Chain R; UniProt 3–150 Not recorded Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-K × 1 (O60814) Histone H2B type 1-K × 1 (O60814) DNA (147-MER) × 1 DNA (147-MER) × 1 E3 ubiquitin-protein ligase BRE1 × 2 (Q07457) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.44 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.

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

View Construct and Data Evidence
UniProt name UBC2_YEAST
Isoform
PDB entities 9
Chains and sequence ranges Author chain R; PDBConstruct 1–148; UniProt 3–150

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 8ieg

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8ieg
Deposition date deposition_date2023-02-15
Structure title titleBre1(mRBD-RING)/Rad6-Ub/nucleosome complex
Keywords keywordsNucleosome, Bre1, Rad6, Ub, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.64
Radius of gyration Rg (electron density) rg_electron39.42
Forward intensity I(0) i01071350000.00
Molecular weight molecular_weight206310.0 kDa
Excluded volume excluded_volume232050 ų
Envelope volume envelope_volume354320 ų
Hydration-shell volume shell_volume72303 ų
Envelope diameter envelope_diameter126.2
Shell Rg shell_rg47.52
Envelope Rg envelope_rg38.58
Shape Rg shape_rg39.30
Total Rg total_rg40.04
Total atoms total_atoms14102
Residues n_residues1329
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 dmax119.7
Rg (real space) rg_real41.37
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real1.0710e+09
I(0) uncertainty (real space) i0_real_error1.7040e+07
Rg (reciprocal space) rg_reciprocal41.64
I(0) (reciprocal space) i0_reciprocal1072000000.0000
Solution quality estimate total_estimate0.8973
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary53.6
Skewness Skewness skewness-0.006
Kurtosis Kurtosis kurtosis-0.656
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha65090000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.978; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.738

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

7. Fold Classification (SCOP + CATH) 7 domains

CATH v4.4 (7 domains)

Domain ID domain_id8iegD01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id8iegE01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id8iegF01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id8iegG01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id8iegH01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id8iegK01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id8iegL01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A

8. Citations (1)

9. Files and Curves (10)