9r2p

p53 bound to nucleosome at position SHL+5.9 (crosslinked sample)

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 12 DNA 2 Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-J × 2 (P06899) DNA-for × 1 DNA-rev × 1 Cellular tumor antigen p53 × 4 (P04637) 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

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 12 DNA 2 Histone H3.1 × 2 (P68431) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-J × 2 (P06899) DNA-for × 1 DNA-rev × 1 Cellular tumor antigen p53 × 4 (P04637) 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

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 12 DNA 2 Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2B type 1-J × 2 (P06899) DNA-for × 1 DNA-rev × 1 Cellular tumor antigen p53 × 4 (P04637) 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

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 12 DNA 2 Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) DNA-for × 1 DNA-rev × 1 Cellular tumor antigen p53 × 4 (P04637) 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 4–128; UniProt 1–125 Author chain H; PDBConstruct 4–128; UniProt 1–125

Cellular tumor antigen p53

Homo sapiens

UniProt P04637

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 12 DNA 2 Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-J × 2 (P06899) DNA-for × 1 DNA-rev × 1 Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name P53_HUMAN
Isoform —
PDB entities 7
Chains and sequence ranges Author chain K; PDBConstruct 25–417; UniProt 1–393 Author chain L; PDBConstruct 25–417; UniProt 1–393 Author chain M; PDBConstruct 25–417; UniProt 1–393 Author chain N; PDBConstruct 25–417; UniProt 1–393

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_id9r2p
Deposition date deposition_date2025-04-30
Structure title titlep53 bound to nucleosome at position SHL+5.9 (crosslinked sample)
Keywords keywordsTumour suppressor, transcription factor, 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.

9r2p__assembly_1__model_1

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

Download this curve (.dat)

9r2p__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.

9r2p__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)53.57 Å
Rg (electron density)53.00 Å
Total Rg52.69 Å
Atom count15460
Residues1821
Excluded volume252480 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 9r2p__assembly_1__model_1 14-meric (14) 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)