SAXSdb — 1jun

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

C-JUN HOMODIMER

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	AP1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–44； UniProt 2–44 Author chain B； PDBConstruct 2–44； UniProt 2–44

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	1jun
Deposition date deposition_date	1995-12-19
Structure title title	NMR STUDY OF C-JUN HOMODIMER
Keywords keywords	TRANSCRIPTION REGULATION, DNA-BINDING REGULATORY PROTEIN, ONCOGENE PROTEIN, TRANSCRIPTION ACTIVATION; TRANSCRIPTION REGULATION
Experimental Method method	SOLUTION NMR

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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.

1jun__assembly_1__model_1

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

Download this curve (.dat)

1jun__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1jun__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	19.90 Å
Rg (electron density)	19.92 Å
Total Rg	20.66 Å
Atom count	1400
Residues	86
Excluded volume	12205 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1jun__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	2	`1jun__assembly_1__model_2`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	3	`1jun__assembly_1__model_3`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	4	`1jun__assembly_1__model_4`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	5	`1jun__assembly_1__model_5`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	6	`1jun__assembly_1__model_6`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	7	`1jun__assembly_1__model_7`	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 (1)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1juna_
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	d1junb_
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	1junA00
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	1junB00
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 (7)

High resolution NMR solution structure of the leucine zipper domain of the c-Jun homodimer.

J.Biol.Chem. (1996)

PMID: 8662824 · DOI: 10.1074/jbc.271.23.13663 PRIMARY

Structural Studies of the Leucine Zipper Domain of the Oncoprotein C-Jun

Thesis (1995)

;Nuclear Magnetic Resonance Characterization of the Jun Leucine Zipper Domain: Unusual Properties of Coiled-Coil Interfacial Polar Residues ;

Biochemistry (1995)

The Solution Structure of the Leucine Zipper Motif of the Jun Oncoprotein Homodimer

Eur.J.Biochem. (1993)

;Determination of the Structure of Symmetric Coiled-Coil Proteins from NMR Data: Application of the Leucine Zipper Proteins Jun and GCN4 ;

Protein Eng. (1993)

Preferential Heterodimer Formation by Isolated Leucine Zippers from Fos and Jun

Science (1989)

;Calculation of Symmetric Multimer Structures from NMR Data Using a Priori Knowledge of the Monomer Structure, Co-Monomer Restraints, and Interface Mapping: The Case of Leucine Zippers ;

To be Published

Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Description description	C-JUN HOMODIMER
Molecular weight formula_weight	4883.7 kDa
Mutation mutation	INS(272-275), INS(315)
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	9800

Source organism organism	Homo sapiens
Common name common_name	human
NCBI taxonomy ID ncbi_taxonomy_id	9606

NMR STUDY OF C-JUN HOMODIMER

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

C-JUN HOMODIMER

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

1jun__assembly_1__model_1

1jun__assembly_1__model_1 | I(q)

1jun__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

5. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (7)

NMR STUDY OF C-JUN HOMODIMER

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

C-JUN HOMODIMER

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

1jun__assembly_1__model_1

1jun__assembly_1__model_1 | I(q)

1jun__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

5. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (7)