8gui

Bre1-nucleosome complex (Model I)

Method: ELECTRON MICROSCOPY Dmax: 119.9 Å Quality: EXCELLENT

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain A; UniProt 1–136 Chain E; UniProt 1–136 Not recorded Histone H4 × 2 (P62805) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-J × 2 (P06899) DNA (147-mer) × 1 DNA (147-mer) × 1 E3 ubiquitin-protein ligase BRE1A × 1 (Q5VTR2) E3 ubiquitin-protein ligase BRE1B × 1 (O75150) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.81 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 A; PDBConstruct 1–136; UniProt 1–136 Author chain E; PDBConstruct 1–136; UniProt 1–136

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain B; UniProt 2–103 Chain F; UniProt 2–103 Not recorded Histone H3.1 × 2 (P68431) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-J × 2 (P06899) DNA (147-mer) × 1 DNA (147-mer) × 1 E3 ubiquitin-protein ligase BRE1A × 1 (Q5VTR2) E3 ubiquitin-protein ligase BRE1B × 1 (O75150) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.81 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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain C; UniProt 2–130 Chain G; UniProt 2–130 Not recorded Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2B type 1-J × 2 (P06899) DNA (147-mer) × 1 DNA (147-mer) × 1 E3 ubiquitin-protein ligase BRE1A × 1 (Q5VTR2) E3 ubiquitin-protein ligase BRE1B × 1 (O75150) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.81 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-J

Homo sapiens

UniProt P06899

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain D; UniProt 1–126 Chain H; UniProt 1–126 Not recorded Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1 × 2 (P0C0S8) DNA (147-mer) × 1 DNA (147-mer) × 1 E3 ubiquitin-protein ligase BRE1A × 1 (Q5VTR2) E3 ubiquitin-protein ligase BRE1B × 1 (O75150) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.81 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.

290 other PDB entries and 301 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1J_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 4–129; UniProt 1–126 Author chain H; PDBConstruct 4–129; UniProt 1–126

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain K; UniProt 1–975 Not recorded Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-J × 2 (P06899) DNA (147-mer) × 1 DNA (147-mer) × 1 E3 ubiquitin-protein ligase BRE1B × 1 (O75150) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.81 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 7
Chains and sequence ranges Author chain K; PDBConstruct 1–975; UniProt 1–975

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain L; UniProt 1–1001 Not recorded Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-J × 2 (P06899) DNA (147-mer) × 1 DNA (147-mer) × 1 E3 ubiquitin-protein ligase BRE1A × 1 (Q5VTR2) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.81 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 8
Chains and sequence ranges Author chain L; PDBConstruct 1–1001; UniProt 1–1001

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 8gui

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8gui
Deposition date deposition_date2022-09-12
Structure title titleBre1-nucleosome complex (Model I)
Keywords keywordstranscription, ubiquitin ligase, cancer, chromatin, GENE REGULATION, GENE REGULATION-DNA complex; GENE REGULATION/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.68
Radius of gyration Rg (electron density) rg_electron38.41
Forward intensity I(0) i0984041000.00
Molecular weight molecular_weight195580.0 kDa
Excluded volume excluded_volume218980 ų
Envelope volume envelope_volume322870 ų
Hydration-shell volume shell_volume67561 ų
Envelope diameter envelope_diameter122.5
Shell Rg shell_rg46.33
Envelope Rg envelope_rg38.00
Shape Rg shape_rg38.26
Total Rg total_rg39.09
Total atoms total_atoms13348
Residues n_residues1214
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 dmax119.9
Rg (real space) rg_real40.45
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real9.8400e+08
I(0) uncertainty (real space) i0_real_error1.7310e+07
Rg (reciprocal space) rg_reciprocal40.67
I(0) (reciprocal space) i0_reciprocal984300000.0000
Solution quality estimate total_estimate0.9007
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary52.2
Skewness Skewness skewness0.033
Kurtosis Kurtosis kurtosis-0.674
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha57390000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.972; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.821

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)