9wc0

The structure of NCP-RA module of ncBAF-nucleosome complex

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

Histone H4

Xenopus laevis

UniProt P62799

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 9 DNA 2 Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) Histone H3.2 × 2 (P84233) DNA (207-MER) × 1 DNA (207-MER) × 1 B-cell CLL/lymphoma 7 protein family member A × 1 (Q4VC05) Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name H4_XENLA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–102; UniProt 2–103 Author chain F; PDBConstruct 1–102; UniProt 2–103

Histone H2A

Xenopus laevis

UniProt Q6AZJ8

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 9 DNA 2 Histone H4 × 2 (P62799) Histone H2B 1.1 × 2 (P02281) Histone H3.2 × 2 (P84233) DNA (207-MER) × 1 DNA (207-MER) × 1 B-cell CLL/lymphoma 7 protein family member A × 1 (Q4VC05) Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name Q6AZJ8_XENLA
Isoform —
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–129; UniProt 2–130 Author chain G; PDBConstruct 1–129; UniProt 2–130

Histone H2B 1.1

Xenopus laevis

UniProt P02281

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 9 DNA 2 Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H3.2 × 2 (P84233) DNA (207-MER) × 1 DNA (207-MER) × 1 B-cell CLL/lymphoma 7 protein family member A × 1 (Q4VC05) Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name H2B11_XENLA
Isoform —
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–125; UniProt 2–126 Author chain H; PDBConstruct 1–125; UniProt 2–126

Histone H3.2

Xenopus laevis

UniProt P84233

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 9 DNA 2 Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (207-MER) × 1 DNA (207-MER) × 1 B-cell CLL/lymphoma 7 protein family member A × 1 (Q4VC05) Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name H32_XENLA
Isoform —
PDB entities 4
Chains and sequence ranges Author chain E; PDBConstruct 1–135; UniProt 2–136 Author chain K; PDBConstruct 1–135; UniProt 2–136

B-cell CLL/lymphoma 7 protein family member A

Homo sapiens

UniProt Q4VC05

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 9 DNA 2 Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) Histone H3.2 × 2 (P84233) DNA (207-MER) × 1 DNA (207-MER) × 1 Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name BCL7A_HUMAN
Isoform —
PDB entities 7
Chains and sequence ranges Author chain O; PDBConstruct 1–210; UniProt 1–210

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_id9wc0
Deposition date deposition_date2025-08-15
Structure title titleThe structure of NCP-RA module of ncBAF-nucleosome complex
Keywords keywordsChromatin remodeling complex, GENE REGULATION/DNA, 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.

9wc0__assembly_1__model_1

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

Download this curve (.dat)

9wc0__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.

9wc0__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)41.51 Å
Rg (electron density)38.72 Å
Total Rg39.42 Å
Atom count12431
Residues1085
Excluded volume201270 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 9wc0__assembly_1__model_1 undecameric (11) 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 (7)

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7. Citations (1)