SAXSdb — 2wp2

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1. Protein Identity and Related Structures Protein Identity & Related Structures

BROMODOMAIN TESTIS-SPECIFIC PROTEIN

MUS MUSCULUS

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	HISTONE H4 × 1 （P62806） water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	HISTONE H4 × 1 （P62806） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	BRDT_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–120； UniProt 17–136 Author chain B； PDBConstruct 1–120； UniProt 17–136

HISTONE H4

OrganismNot specified

UniProt P62806

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	BROMODOMAIN TESTIS-SPECIFIC PROTEIN × 1 （Q91Y44） water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	BROMODOMAIN TESTIS-SPECIFIC PROTEIN × 1 （Q91Y44） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	H4_MOUSE
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain P； PDBConstruct 1–20； UniProt 2–21 Author chain Q； PDBConstruct 1–20； UniProt 2–21

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_id	2wp2
Deposition date deposition_date	2009-08-02
Structure title title	Structure of Brdt bromodomain BD1 bound to a diacetylated histone H4 peptide.
Keywords keywords	TRANSCRIPTION-PEPTIDE COMPLEX, TRANSCRIPTION REGULATION, BRDT, ACETYLLYSINE, NUCLEUS, COILED COIL, CHROMOSOMAL PROTEIN, NUCLEOSOME; TRANSCRIPTION/PEPTIDE
Experimental Method method	X-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.

2wp2__assembly_1__model_1

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

Download this curve (.dat)

2wp2__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2wp2__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	15.99 Å
Rg (electron density)	14.76 Å
Total Rg	15.96 Å
Atom count	996
Residues	122
Excluded volume	17961 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2wp2__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2wp2__assembly_2__model_1`	dimeric （2）	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 (3)

Entity 1 Entity 1 polymer

Description description	BROMODOMAIN TESTIS-SPECIFIC PROTEIN
Molecular weight formula_weight	14271.5 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	2099

EYINTKKSGRLTNQLQFLQRVVLKALWKHGFSWPFQQPVDAVKLKLPDYYTIIKTPMDLNTIKKRLENKYYEKASECIEDFNTMFSNCYLYNKTGDDIVVMAQALEKLFMQKLSQMPQEE

Source Source

Source organism organism	MUS MUSCULUS
Common name common_name	MOUSE
NCBI taxonomy ID ncbi_taxonomy_id	10090
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	HISTONE H4
Molecular weight formula_weight	2083.4 kDa
Source method src_method	syn
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	P,Q

SGRGKGGKGLGKGGAKRHRK

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	111

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6. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id	2wp2A01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	920 — Histone Acetyltransferase; Chain A
Homologous superfamily homologous superfamily	10 — Bromodomain-like

Domain ID domain_id	2wp2B01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	920 — Histone Acetyltransferase; Chain A
Homologous superfamily homologous superfamily	10 — Bromodomain-like

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Unit-cell length a length_a	49.293 Å
Unit-cell length b length_b	61.224 Å
Unit-cell length c length_c	97.910 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.370 Å
Low-resolution limit resolution_low	44.000 Å
R factor r_factor	0.2170
R_work r_work	0.2170
R_free r_free	0.2610

Structure of Brdt bromodomain BD1 bound to a diacetylated histone H4 peptide.

1. Protein Identity and Related Structures Protein Identity & Related Structures

BROMODOMAIN TESTIS-SPECIFIC PROTEIN

State in the Current Structure

Other States of the Same Protein in the Database

HISTONE H4

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

2wp2__assembly_1__model_1

2wp2__assembly_1__model_1 | I(q)

2wp2__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

7. Citations (1)

Structure of Brdt bromodomain BD1 bound to a diacetylated histone H4 peptide.

1. Protein Identity and Related Structures Protein Identity & Related Structures

BROMODOMAIN TESTIS-SPECIFIC PROTEIN

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

HISTONE H4

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

2wp2__assembly_1__model_1

2wp2__assembly_1__model_1 | I(q)

2wp2__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

7. Citations (1)