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	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 2–44 Chain B； UniProt 2–44	Fragment：LEUCINE ZIPPER DOMAIN, RESIDUES 272 - 315 Mutation：INS(272-275), INS(315) Non-standard monomer：Yes (specific site not provided by mmCIF)	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 3.6；310 K	Resolution not provided

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 1JUN	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1A02 STRUCTURE OF THE DNA BINDING DOMAINS OF NFAT, FOS AND JUN BOUND TO DNA Deposited 1997-12-08	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 3 PDB declaration: pentameric	Chain J 253–308（56 aa） Fragment：JUN	Mutation：C279S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；THE COMPLEX WAS CRYSTALLIZED IN 300-400 MM AMMONIUM ACETATE SALT, PH 7.5 (10 MM)., VAPOR DIFFUSION, HANGING DROP	Resolution 2.70 Å R-free 0.303
1JNM Crystal Structure of the Jun/CRE Complex Deposited 2001-07-24	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric	Chain A 254–315（62 aa） Fragment：bZIP domain Chain B 254–315（62 aa） Fragment：bZIP domain	Mutation：C269S Mutation：C269S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；PEG 4000, Cacodylate, sodium chloride, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.20 Å R-free 0.286
1S9K Crystal Structure of Human NFAT1 and Fos-Jun on the IL-2 ARRE1 Site Deposited 2004-02-04	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 3 PDB declaration: pentameric	Chain E 257–308（52 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；289 K；300-400 mM Ammonium Acetate Salt, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 3.10 Å R-free 0.275
1T2K Structure Of The DNA Binding Domains Of IRF3, ATF-2 and Jun Bound To DNA Deposited 2004-04-21	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 4 PDB declaration: hexameric	Chain C 254–314（61 aa） Fragment：bZip domain	Mutation：C269S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；295 K；100 mM NaCacodylate, pH 6.5, 12.5% (w/v) PEG 6000, 400 mM NH4OAc, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 3.00 Å R-free 0.296
5T01 Human c-Jun DNA binding domain homodimer in complex with methylated DNA Deposited 2016-08-15	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric	Chain A 254–315（62 aa） Fragment：DNA binding domain (UNP residues 254-315) Chain B 254–315（62 aa） Fragment：DNA binding domain (UNP residues 254-315)	Mutation：C269S Mutation：C269S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；289 K；0.05 M Citric acid 0.05 M Bis-Tris propane 16% PEG3350	Resolution 1.89 Å R-free 0.227

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

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. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	19.65 Å
Radius of gyration Rg (electron density) rg_electron	19.95 Å
Forward intensity I(0) i0	73826200.00
Molecular weight molecular_weight	68555.0 kDa
Excluded volume excluded_volume	85434 Å³
Envelope volume envelope_volume	27020 Å³
Hydration-shell volume shell_volume	11806 Å³
Envelope diameter envelope_diameter	76.2 Å
Shell Rg shell_rg	26.19 Å
Envelope Rg envelope_rg	22.87 Å
Shape Rg shape_rg	19.89 Å
Total Rg total_rg	20.43 Å
Total atoms total_atoms	9800
Residues n_residues	602
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	53.6 Å
Rg (real space) rg_real	18.28 Å
Rg uncertainty (real space) rg_real_error	0.13 Å
I(0) (real space) i0_real	7.0440e+07
I(0) uncertainty (real space) i0_real_error	6.7220e+05
Rg (reciprocal space) rg_reciprocal	20.10 Å
I(0) (reciprocal space) i0_reciprocal	73820000.0000
Solution quality estimate total_estimate	0.6465
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	0
Primary peak position r_peak_primary	— Å
Skewness Skewness skewness	0.430
Kurtosis Kurtosis kurtosis	-0.649
Angular range angular_range	— – 0.4050 Å⁻¹
Current regularization parameter α current_alpha	2.8000
Highest regularization parameter α highest_alpha	81940.0000
Real-space data points n_real_points	72
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.001; Oscil: 0.947; Stabil: 0.981; Sysdev: 0.000; Positv: 1.000; Valcen: 0.640; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. 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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8. 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

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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

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 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

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

8. Citations (7)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/ju/1jun/1jun.fit
pddf	/app/data/pr_computation/ju/1jun/1jun.pr.out
profile	/app/data/saxs_computation/ju/1jun/1jun.dat