6l4a

H3-H3-H3 tri-nucleosome with the 22 base-pair linker DNA

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 24 DNA 2 Histone H4 × 6 (P62805) Histone H2A type 1-B/E × 6 (P04908) Histone H2B type 1-J × 6 (P06899) DNA (485-MER) × 1 DNA (485-MER) × 1 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 4–139; UniProt 1–136 Author chain E; PDBConstruct 4–139; UniProt 1–136 Author chain K; PDBConstruct 4–139; UniProt 1–136 Author chain O; PDBConstruct 4–139; UniProt 1–136 Author chain S; PDBConstruct 4–139; UniProt 1–136 Author chain W; PDBConstruct 4–139; 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 24 DNA 2 Histone H3.1 × 6 (P68431) Histone H2A type 1-B/E × 6 (P04908) Histone H2B type 1-J × 6 (P06899) DNA (485-MER) × 1 DNA (485-MER) × 1 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 4–106; UniProt 1–103 Author chain F; PDBConstruct 4–106; UniProt 1–103 Author chain L; PDBConstruct 4–106; UniProt 1–103 Author chain P; PDBConstruct 4–106; UniProt 1–103 Author chain T; PDBConstruct 4–106; UniProt 1–103 Author chain X; PDBConstruct 4–106; UniProt 1–103

Histone H2A type 1-B/E

Homo sapiens

UniProt P04908

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 24 DNA 2 Histone H3.1 × 6 (P68431) Histone H4 × 6 (P62805) Histone H2B type 1-J × 6 (P06899) DNA (485-MER) × 1 DNA (485-MER) × 1 Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name H2A1B_HUMAN
Isoform —
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 4–133; UniProt 1–130 Author chain G; PDBConstruct 4–133; UniProt 1–130 Author chain M; PDBConstruct 4–133; UniProt 1–130 Author chain Q; PDBConstruct 4–133; UniProt 1–130 Author chain U; PDBConstruct 4–133; UniProt 1–130 Author chain Y; PDBConstruct 4–133; UniProt 1–130

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 24 DNA 2 Histone H3.1 × 6 (P68431) Histone H4 × 6 (P62805) Histone H2A type 1-B/E × 6 (P04908) DNA (485-MER) × 1 DNA (485-MER) × 1 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 Author chain N; PDBConstruct 4–129; UniProt 1–126 Author chain R; PDBConstruct 4–129; UniProt 1–126 Author chain V; PDBConstruct 4–129; UniProt 1–126 Author chain Z; PDBConstruct 4–129; UniProt 1–126

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_id6l4a
Deposition date deposition_date2019-10-16
Structure title titleH3-H3-H3 tri-nucleosome with the 22 base-pair linker DNA
Keywords keywordsChromatin, Nucleosome, Centromere, NUCLEAR PROTEIN; NUCLEAR PROTEIN
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.

6l4a__assembly_1__model_1

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

Download this curve (.dat)

6l4a__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 109 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

6l4a__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)86.99 Å
Rg (electron density)87.45 Å
Total Rg87.42 Å
Atom count37756
Residues3223
Excluded volume609760 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 6l4a__assembly_1__model_1 26-meric (26) 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 (6)

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7. Citations (1)