9l1x

hDEK-nucleosome complex (conformation 1)

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

Histone H3.3

Homo sapiens

UniProt P84243

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-B/E × 2 (P04908) Histone H2B type 1-J × 2 (P06899) 601 DNA_R (189-MER) × 1 601 DNA (189-MER) × 1 Protein DEK × 2 (P35659) UNKNOWN ATOM OR ION × 2 Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name H33_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 10 DNA 2 Histone H3.3 × 2 (P84243) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-J × 2 (P06899) 601 DNA_R (189-MER) × 1 601 DNA (189-MER) × 1 Protein DEK × 2 (P35659) UNKNOWN ATOM OR ION × 2 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-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 10 DNA 2 Histone H3.3 × 2 (P84243) Histone H4 × 2 (P62805) Histone H2B type 1-J × 2 (P06899) 601 DNA_R (189-MER) × 1 601 DNA (189-MER) × 1 Protein DEK × 2 (P35659) UNKNOWN ATOM OR ION × 2 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 1–119; UniProt 2–120 Author chain G; PDBConstruct 1–119; UniProt 2–120

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 H3.3 × 2 (P84243) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) 601 DNA_R (189-MER) × 1 601 DNA (189-MER) × 1 Protein DEK × 2 (P35659) UNKNOWN ATOM OR ION × 2 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 1–125; UniProt 2–126 Author chain H; PDBConstruct 1–125; UniProt 2–126

Protein DEK

Homo sapiens

UniProt P35659

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 H3.3 × 2 (P84243) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-J × 2 (P06899) 601 DNA_R (189-MER) × 1 601 DNA (189-MER) × 1 UNKNOWN ATOM OR ION × 2 Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name DEK_HUMAN
Isoform —
PDB entities 7
Chains and sequence ranges Author chain K; PDBConstruct 1–375; UniProt 1–375 Author chain L; PDBConstruct 1–375; UniProt 1–375

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_id9l1x
Deposition date deposition_date2024-12-16
Structure title titlehDEK-nucleosome complex (conformation 1)
Keywords keywordsnucleosome complex, GENE REGULATION; GENE REGULATION
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.

Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 9l1x__assembly_1__model_1 dodecameric (12) Excluded — —
Exclusion reason: The source record does not identify the atom or ion element unambiguously, so a reliable calculation is not possible.
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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)