9nqu

KDM6B-nucleosome structure stabilized by H3K27C-UNC8015 covalent conjugate

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

Histone H3.2

Homo sapiens

UniProt Q71DI3

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 (P62805) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-C/E/F/G/I × 2 (P62807) DNA (185-MER) × 1 DNA (185-MER) × 1 Lysine-specific demethylase 6B × 1 (Q5NCY0) FE (III) ION × 1 ZINC ION × 1 N-heptanoyl-N-hydroxy-beta-alanine × 1 Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name H32_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–135; UniProt 2–136 Author chain E; PDBConstruct 1–135; UniProt 2–136

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 9 DNA 2 Histone H3.2 × 2 (Q71DI3) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-C/E/F/G/I × 2 (P62807) DNA (185-MER) × 1 DNA (185-MER) × 1 Lysine-specific demethylase 6B × 1 (Q5NCY0) FE (III) ION × 1 ZINC ION × 1 N-heptanoyl-N-hydroxy-beta-alanine × 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 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 9 DNA 2 Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2B type 1-C/E/F/G/I × 2 (P62807) DNA (185-MER) × 1 DNA (185-MER) × 1 Lysine-specific demethylase 6B × 1 (Q5NCY0) FE (III) ION × 1 ZINC ION × 1 N-heptanoyl-N-hydroxy-beta-alanine × 1 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-C/E/F/G/I

Homo sapiens

UniProt P62807

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 H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2A type 1 × 2 (P0C0S8) DNA (185-MER) × 1 DNA (185-MER) × 1 Lysine-specific demethylase 6B × 1 (Q5NCY0) FE (III) ION × 1 ZINC ION × 1 N-heptanoyl-N-hydroxy-beta-alanine × 1 Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name H2B1C_HUMAN
Isoform —
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–125; UniProt 2–126 Author chain H; PDBConstruct 1–125; UniProt 2–126

Lysine-specific demethylase 6B

Mus musculus

UniProt Q5NCY0

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 H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-C/E/F/G/I × 2 (P62807) DNA (185-MER) × 1 DNA (185-MER) × 1 FE (III) ION × 1 ZINC ION × 1 N-heptanoyl-N-hydroxy-beta-alanine × 1 Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name KDM6B_MOUSE
Isoform —
PDB entities 7
Chains and sequence ranges Author chain K; PDBConstruct 3–514; UniProt 1130–1641

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_id9nqu
Deposition date deposition_date2025-03-13
Structure title titleKDM6B-nucleosome structure stabilized by H3K27C-UNC8015 covalent conjugate
Keywords keywordshistone H3K27 demethylation, GENE REGULATION, histone, chromatin, epigenetics, 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.

9nqu__assembly_1__model_1

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

Download this curve (.dat)

9nqu__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.

9nqu__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)50.04 Å
Rg (electron density)49.14 Å
Total Rg49.38 Å
Atom count17358
Residues1599
Excluded volume284900 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 9nqu__assembly_1__model_1 11-meric (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 (10)

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7. Citations (1)