9si9

Chromosomal Passenger Complex in complex with H3T3ph Nucleosome (Class0)

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

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 12 DNA 2 DNA (147-MER) × 1 DNA (147-MER) × 1 Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-J × 2 (P06899) Borealin × 2 (Q53HL2) Baculoviral IAP repeat-containing protein 5 × 1 (O15392) Inner centromere protein × 1 (Q9NQS7) H3.4 histone × 1 (S4RAZ3) 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 3
Chains and sequence ranges Author chain A; PDBConstruct 1–135; UniProt 2–136

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 12 DNA 2 DNA (147-MER) × 1 DNA (147-MER) × 1 Histone H3.2 × 1 (P84233) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-J × 2 (P06899) Borealin × 2 (Q53HL2) Baculoviral IAP repeat-containing protein 5 × 1 (O15392) Inner centromere protein × 1 (Q9NQS7) H3.4 histone × 1 (S4RAZ3) 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 4
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 12 DNA 2 DNA (147-MER) × 1 DNA (147-MER) × 1 Histone H3.2 × 1 (P84233) Histone H4 × 2 (P62799) Histone H2B type 1-J × 2 (P06899) Borealin × 2 (Q53HL2) Baculoviral IAP repeat-containing protein 5 × 1 (O15392) Inner centromere protein × 1 (Q9NQS7) H3.4 histone × 1 (S4RAZ3) 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 5
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-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 DNA (147-MER) × 1 DNA (147-MER) × 1 Histone H3.2 × 1 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P0C0S8) Borealin × 2 (Q53HL2) Baculoviral IAP repeat-containing protein 5 × 1 (O15392) Inner centromere protein × 1 (Q9NQS7) H3.4 histone × 1 (S4RAZ3) 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 6
Chains and sequence ranges Author chain D; PDBConstruct 1–125; UniProt 2–126 Author chain H; PDBConstruct 1–125; UniProt 2–126

Borealin

Homo sapiens

UniProt Q53HL2

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 DNA (147-MER) × 1 DNA (147-MER) × 1 Histone H3.2 × 1 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-J × 2 (P06899) Baculoviral IAP repeat-containing protein 5 × 1 (O15392) Inner centromere protein × 1 (Q9NQS7) H3.4 histone × 1 (S4RAZ3) Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name BOREA_HUMAN
Isoform —
PDB entities 7
Chains and sequence ranges Author chain L; PDBConstruct 1–280; UniProt 1–280 Author chain O; PDBConstruct 1–280; UniProt 1–280

Baculoviral IAP repeat-containing protein 5

Homo sapiens

UniProt O15392

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 DNA (147-MER) × 1 DNA (147-MER) × 1 Histone H3.2 × 1 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-J × 2 (P06899) Borealin × 2 (Q53HL2) Inner centromere protein × 1 (Q9NQS7) H3.4 histone × 1 (S4RAZ3) Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name BIRC5_HUMAN
Isoform —
PDB entities 8
Chains and sequence ranges Author chain M; PDBConstruct 1–142; UniProt 1–142

Inner centromere protein

Homo sapiens

UniProt Q9NQS7

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 DNA (147-MER) × 1 DNA (147-MER) × 1 Histone H3.2 × 1 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-J × 2 (P06899) Borealin × 2 (Q53HL2) Baculoviral IAP repeat-containing protein 5 × 1 (O15392) H3.4 histone × 1 (S4RAZ3) Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name INCE_HUMAN
Isoform —
PDB entities 9
Chains and sequence ranges Author chain N; PDBConstruct 1–918; UniProt 1–918

H3.4 histone

Homo sapiens

UniProt S4RAZ3

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 DNA (147-MER) × 1 DNA (147-MER) × 1 Histone H3.2 × 1 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-J × 2 (P06899) Borealin × 2 (Q53HL2) Baculoviral IAP repeat-containing protein 5 × 1 (O15392) Inner centromere protein × 1 (Q9NQS7) Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name S4RAZ3_PETMA
Isoform —
PDB entities 10
Chains and sequence ranges Author chain E; PDBConstruct 1–135; UniProt 25–159

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_id9si9
Deposition date deposition_date2025-08-28
Structure title titleChromosomal Passenger Complex in complex with H3T3ph Nucleosome (Class0)
Keywords keywordsNucleosome-binding DNA-binding Stabilising Nucleosome Acidic-patch interaction, CELL CYCLE; CELL CYCLE
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.

9si9__assembly_1__model_1

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

Download this curve (.dat)

9si9__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.

9si9__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)43.41 Å
Rg (electron density)42.33 Å
Total Rg42.70 Å
Atom count14471
Residues1346
Excluded volume239030 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 9si9__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 (10)

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7. Citations (1)