SAXSdb — 1gu4

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

CAAT/ENHANCER BINDING PROTEIN BETA

HOMO SAPIENS

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–DNA	Homooligomer	Protein 2 DNA 2	;5'-D(TPAPGPGPAPTPTPGPCPGP* CPAPAPTPAPT)-3' ; × 1 ;5'-D(APAPTPAPTPTPGPCPGPCP APAPTPCPCP*T)-3' ; × 1 water × 4	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	P17676
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–78； UniProt 259–336 Author chain B； PDBConstruct 1–78； UniProt 259–336

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	1gu4
Deposition date deposition_date	2002-01-23
Structure title title	Crystal structure of C/EBPBETA BZIP homodimer bound to a high affinity DNA fragment
Keywords keywords	TRANSCRIPTION/DNA, PROTEIN-DNA COMPLEX, TRANSCRIPTION FACTOR, BZIP, C/EBP, HYPOTHETICAL PROTEIN, TRANSCRIPTION-DNA complex; TRANSCRIPTION/DNA
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.

1gu4__assembly_1__model_1

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

Download this curve (.dat)

1gu4__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1gu4__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	25.75 Å
Rg (electron density)	27.66 Å
Total Rg	27.64 Å
Atom count	1779
Residues	166
Excluded volume	29459 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1gu4__assembly_1__model_1`	tetrameric （4）	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 (4)

Entity 1 Entity 1 polymer

Description description	CAAT/ENHANCER BINDING PROTEIN BETA
Molecular weight formula_weight	9381.9 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	2090

VKSKAKKTVDKHSDEYKIRRERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQLSRELSTLRNLFKQLPE

Source Source

Source organism organism	HOMO SAPIENS
Common name common_name	HUMAN
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	;5'-D(TPAPGPGPAPTPTPGPCPGP* CPAPAPTPAP*T)-3' ;
Molecular weight formula_weight	4937.2 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polydeoxyribonucleotide
Chain IDs strand_id	C

TAGGATTGCGCAATAT

Entity 3 Entity 3 polymer

Description description	;5'-D(APAPTPAPTPTPGPCPGPCP* APAPTPCPCP*T)-3' ;
Molecular weight formula_weight	4857.2 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polydeoxyribonucleotide
Chain IDs strand_id	D

AATATTGCGCAATCCT

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	311

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1gu4a_
Class class	h — Coiled coil proteins
Fold Fold fold	h.1 — Parallel coiled-coil
Superfamily Superfamily superfamily	h.1.3 — Leucine zipper domain
Family Family family	h.1.3.1 — Leucine zipper domain

Domain ID domain_id	d1gu4b_
Class class	h — Coiled coil proteins
Fold Fold fold	h.1 — Parallel coiled-coil
Superfamily Superfamily superfamily	h.1.3 — Leucine zipper domain
Family Family family	h.1.3.1 — Leucine zipper domain

CATH v4.4 (2 domains)

Domain ID domain_id	1gu4A00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	170 —

Domain ID domain_id	1gu4B00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	170 —

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7. Citations (6)

Structural Basis for Flexible Base Recognition by C/Ebpbeta

To be Published

PRIMARY

Mechanism of C-Myb-C/Ebpbeta Cooperation from Separated Sites on a Promoter

Cell (Cambridge,Mass.) (2002)

PMID: 11792321 · DOI: 10.1016/S0092-8674(01)00636-5

Crystallization and Preliminary X-Ray Analysis of the C/Ebpbeta C-Terminal Region in Complex with DNA

Acta Crystallogr.,Sect.D (2001)

PMID: 11375506 · DOI: 10.1107/S0907444901003912

Structural Analyses of DNA Recognition by the Aml1/ Runx-1 Runt Domain and its Allosteric Control by Cbfbeta

Cell (Cambridge,Mass.) (2001)

PMID: 11257229 · DOI: 10.1016/S0092-8674(01)00271-9

;Crystallization and Preliminary X-Ray Analyses of Quaternary, Ternary and Binary Protein-DNA Complexes with Involvement of Aml1/Runx-1/Cbfalpha Runt Domain, Cbfbeta and the C/Ebpbeta bZIP Region ;

Acta Crystallogr.,Sect.D (2001)

PMID: 11375505 · DOI: 10.1107/S0907444901003900

;Crystals of Ternary Protein-DNA Complexes Composed of DNA-Binding Domains C-Myb or V-Myb, C/Ebpalpha or C/Ebpbeta and Tom-1A Promoter Fragment ;

Acta Crystallogr.,Sect.D (2001)

PMID: 11679735 · DOI: 10.1107/S0907444901011982

Unit-cell length a length_a	100.947 Å
Unit-cell length b length_b	112.326 Å
Unit-cell length c length_c	74.401 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	16

Space group space_group	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	—

Resolution resolution	1.800 Å
Low-resolution limit resolution_low	29.950 Å
R factor r_factor	0.2320
R_work r_work	0.2320
R_free r_free	0.2660

Crystal structure of C/EBPBETA BZIP homodimer bound to a high affinity DNA fragment

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

CAAT/ENHANCER BINDING PROTEIN BETA

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

1gu4__assembly_1__model_1

1gu4__assembly_1__model_1 | I(q)

1gu4__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (6)

Crystal structure of C/EBPBETA BZIP homodimer bound to a high affinity DNA fragment

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

CAAT/ENHANCER BINDING PROTEIN BETA

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

1gu4__assembly_1__model_1

1gu4__assembly_1__model_1 | I(q)

1gu4__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (6)