8guj

Bre1-nucleosome complex (Model II)

Method: ELECTRON MICROSCOPY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Histone H3.1

Homo sapiens

UniProt P68431

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 10 DNA 2 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) ZINC ION × 4 Consistent with all polymers

Other States of the Same Protein in the Database

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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 10 DNA 2 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) ZINC ION × 4 Consistent with all polymers

Other States of the Same Protein in the Database

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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 10 DNA 2 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) ZINC ION × 4 Consistent with all polymers

Other States of the Same Protein in the Database

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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 10 DNA 2 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) ZINC ION × 4 Consistent with all polymers

Other States of the Same Protein in the Database

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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 10 DNA 2 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) ZINC ION × 4 Consistent with all polymers

Other States of the Same Protein in the Database

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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 10 DNA 2 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) ZINC ION × 4 Consistent with all polymers

Other States of the Same Protein in the Database

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id8guj
Deposition date deposition_date2022-09-12
Structure title titleBre1-nucleosome complex (Model II)
Keywords keywordstranscription, ubiquitin ligase, cancer, chromatin, GENE REGULATION, GENE REGULATION-DNA complex; GENE REGULATION/DNA
Experimental Method methodELECTRON MICROSCOPY
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

8guj__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

8guj__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

8guj__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)40.68 Å
Rg (electron density)38.42 Å
Total Rg39.11 Å
Atom count13348
Residues1214
Excluded volume218980 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 8guj__assembly_1__model_1 dodecameric (12) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (9)

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7. Citations (1)