8evj

CX3CR1 nucleosome bound PU.1 and C/EBPa

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 11 DNA 2 DNA (167-MER) × 1 DNA (167-MER) × 1 Histone H4 × 2 (P62805) Histone H2A type 2-C × 2 (Q16777) Histone H2B type 2-E × 2 (Q16778) ScFv × 2 Transcription factor PU.1 × 1 (P17433) 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 3
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 11 DNA 2 DNA (167-MER) × 1 DNA (167-MER) × 1 Histone H3.1 × 2 (P68431) Histone H2A type 2-C × 2 (Q16777) Histone H2B type 2-E × 2 (Q16778) ScFv × 2 Transcription factor PU.1 × 1 (P17433) 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 4
Chains and sequence ranges Author chain B; PDBConstruct 1–103; UniProt 1–103 Author chain F; PDBConstruct 1–103; UniProt 1–103

Histone H2A type 2-C

Homo sapiens

UniProt Q16777

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 11 DNA 2 DNA (167-MER) × 1 DNA (167-MER) × 1 Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2B type 2-E × 2 (Q16778) ScFv × 2 Transcription factor PU.1 × 1 (P17433) Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name H2A2C_HUMAN
Isoform —
PDB entities 5
Chains and sequence ranges Author chain C; PDBConstruct 1–129; UniProt 1–129 Author chain G; PDBConstruct 1–129; UniProt 1–129

Histone H2B type 2-E

Homo sapiens

UniProt Q16778

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 11 DNA 2 DNA (167-MER) × 1 DNA (167-MER) × 1 Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 2-C × 2 (Q16777) ScFv × 2 Transcription factor PU.1 × 1 (P17433) Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name H2B2E_HUMAN
Isoform —
PDB entities 6
Chains and sequence ranges Author chain D; PDBConstruct 1–126; UniProt 1–126 Author chain H; PDBConstruct 1–126; UniProt 1–126

Transcription factor PU.1

Mus musculus

UniProt P17433

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 11 DNA 2 DNA (167-MER) × 1 DNA (167-MER) × 1 Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 2-C × 2 (Q16777) Histone H2B type 2-E × 2 (Q16778) ScFv × 2 Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name SPI1_MOUSE
Isoform —
PDB entities 8
Chains and sequence ranges Author chain O; PDBConstruct 14–285; UniProt 1–272

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_id8evj
Deposition date deposition_date2022-10-20
Structure title titleCX3CR1 nucleosome bound PU.1 and C/EBPa
Keywords keywords;nucleosome, transcription factor, transcription, CHROMATIN BINDING PROTEIN-DNA complex, DNA BINDING PROTEIN, TRANSCRIPTION-DNA complex ;; TRANSCRIPTION/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.

8evj__assembly_1__model_1

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

Download this curve (.dat)

8evj__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.

8evj__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)44.90 Å
Rg (electron density)42.84 Å
Total Rg43.38 Å
Atom count15951
Residues1577
Excluded volume266560 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 8evj__assembly_1__model_1 13-meric (13) 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 (8)

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7. Citations (1)