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4h9s

Complex structure 6 of DAXX/H3.3(sub7)/H4

Method: X-RAY DIFFRACTION
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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 heterocomplex Heteromer Protein 3 Histone H4 × 1 （P62805） Death domain-associated protein 6 × 1 （Q9UER7） PHOSPHATE ION × 3 water × 3 Consistent with protein count
2 Protein heterocomplex Heteromer Protein 3 Histone H4 × 1 （P62805） Death domain-associated protein 6 × 1 （Q9UER7） PHOSPHATE ION × 2 water × 3 Consistent with protein count
3 Protein heterocomplex Heteromer Protein 6 Histone H4 × 2 （P62805） Death domain-associated protein 6 × 2 （Q9UER7） PHOSPHATE ION × 5 water × 6 Consistent with protein count

Other States of the Same Protein in the Database

Monomer

None

Homodimer

None

Homotetramer

None

Other homooligomers

None

Heteromeric or nucleic-acid complex
2l43 3ask 3ask 3ask 3asl 3av2 3jvk 3muk 3mul 3ql9 3qla 3qla

124 assemblies; showing the first 12

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 B； 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 heterocomplex Heteromer Protein 3 Histone H3.3 × 1 （P84243） Death domain-associated protein 6 × 1 （Q9UER7） PHOSPHATE ION × 3 water × 3 Consistent with protein count
2 Protein heterocomplex Heteromer Protein 3 Histone H3.3 × 1 （P84243） Death domain-associated protein 6 × 1 （Q9UER7） PHOSPHATE ION × 2 water × 3 Consistent with protein count
3 Protein heterocomplex Heteromer Protein 6 Histone H3.3 × 2 （P84243） Death domain-associated protein 6 × 2 （Q9UER7） PHOSPHATE ION × 5 water × 6 Consistent with protein count

Other States of the Same Protein in the Database

Monomer

None

Homodimer

None

Homotetramer

None

Other homooligomers

None

Heteromeric or nucleic-acid complex
10xz 10ya 10yb 10yc 10yd 10ye 10yf 10yg 10yh 10yi 2bqz 2bqz

634 assemblies; showing the first 12

View Construct and Data Evidence
UniProt name H4_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain C； PDBConstruct 1–83； UniProt 21–103 Author chain D； PDBConstruct 1–83； UniProt 21–103

Death domain-associated protein 6

Homo sapiens

UniProt Q9UER7

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 3 Histone H3.3 × 1 （P84243） Histone H4 × 1 （P62805） PHOSPHATE ION × 3 water × 3 Consistent with protein count
2 Protein heterocomplex Heteromer Protein 3 Histone H3.3 × 1 （P84243） Histone H4 × 1 （P62805） PHOSPHATE ION × 2 water × 3 Consistent with protein count
3 Protein heterocomplex Heteromer Protein 6 Histone H3.3 × 2 （P84243） Histone H4 × 2 （P62805） PHOSPHATE ION × 5 water × 6 Consistent with protein count

Other States of the Same Protein in the Database

Monomer

None

Homodimer

None

Homotetramer

None

Other homooligomers

None

Heteromeric or nucleic-acid complex
2kqs 4h9n 4h9o 4h9p 4h9p 4h9q 4h9q 4h9r 4h9r 4h9s 4h9s 4h9s

19 assemblies; showing the first 12

View Construct and Data Evidence
UniProt name DAXX_HUMAN
Isoform —
PDB entities 3
Chains and sequence ranges Author chain E； PDBConstruct 1–216； UniProt 183–398 Author chain F； PDBConstruct 1–216； UniProt 183–398

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_id4h9s
Deposition date deposition_date2012-09-24
Structure title titleComplex structure 6 of DAXX/H3.3(sub7)/H4
Keywords keywordshistone chaperone, DNA BINDING PROTEIN-APOPTOSIS complex; DNA BINDING PROTEIN/APOPTOSIS
Experimental Method methodX-RAY DIFFRACTION
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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.

4h9s__assembly_1__model_1

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

Download this curve (.dat)

4h9s__assembly_1__model_1 | I(q)

10-2 10-1 105 106 107 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

4h9s__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）23.86 Å
Rg (electron density)22.79 Å
Total Rg23.69 Å
Atom count2962
Residues366
Excluded volume52649 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 4h9s__assembly_1__model_1 trimeric （3） Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 4h9s__assembly_2__model_1 trimeric （3） Success 4.1.3-1-20251215 (887e7ef) View Download
3 1 4h9s__assembly_3__model_1 hexameric （6） 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 (5)

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6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd4h9sa_
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.1 — Nucleosome core histones
Domain ID domain_idd4h9sb_
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.1 — Nucleosome core histones
Domain ID domain_idd4h9sc_
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.1 — Nucleosome core histones
Domain ID domain_idd4h9sd_
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.1 — Nucleosome core histones

CATH v4.4 (6 domains)

Domain ID domain_id4h9sA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4h9sB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4h9sC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4h9sD00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4h9sE00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily2170 —
Domain ID domain_id4h9sF00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily2170 —
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7. Citations (1)