SAXSdb — 1a02

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

NUCLEAR FACTOR OF ACTIVATED T CELLS

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–DNA	Heteromer	Protein 3 DNA 2	;DNA (5'-D(DTPDTPDGPDGPDAPDAPDAPDAPDTPDTPDTPDGPDTPDTPDTPDCPDAPDTPDAPDG)-3') ; × 1 ;DNA (5'-D(DAPDAPDCPDTPDAPDTPDGPDAPDAPDAPDCPDAPDAPDAPDTPDTPDTPDTPDCPDC)-3') ; × 1 AP-1 FRAGMENT FOS × 1 （P01100） AP-1 FRAGMENT JUN × 1 （P05412） water × 5	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	NFAC2_HUMAN
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain N； PDBConstruct 19–301； UniProt 396–678

AP-1 FRAGMENT FOS

Homo sapiens

UniProt P01100

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–DNA	Heteromer	Protein 3 DNA 2	;DNA (5'-D(DTPDTPDGPDGPDAPDAPDAPDAPDTPDTPDTPDGPDTPDTPDTPDCPDAPDTPDAPDG)-3') ; × 1 ;DNA (5'-D(DAPDAPDCPDTPDAPDTPDGPDAPDAPDAPDCPDAPDAPDAPDTPDTPDTPDTPDCPDC)-3') ; × 1 NUCLEAR FACTOR OF ACTIVATED T CELLS × 1 （Q13469） AP-1 FRAGMENT JUN × 1 （P05412） water × 5	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FOS_HUMAN
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain F； PDBConstruct 1–56； UniProt 138–193

AP-1 FRAGMENT JUN

Homo sapiens

UniProt P05412

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–DNA	Heteromer	Protein 3 DNA 2	;DNA (5'-D(DTPDTPDGPDGPDAPDAPDAPDAPDTPDTPDTPDGPDTPDTPDTPDCPDAPDTPDAPDG)-3') ; × 1 ;DNA (5'-D(DAPDAPDCPDTPDAPDTPDGPDAPDAPDAPDCPDAPDAPDAPDTPDTPDTPDTPDCPDC)-3') ; × 1 NUCLEAR FACTOR OF ACTIVATED T CELLS × 1 （Q13469） AP-1 FRAGMENT FOS × 1 （P01100） water × 5	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	AP1_HUMAN
Isoform	—
PDB entities	5
Chains and sequence ranges	Author chain J； PDBConstruct 1–56； UniProt 253–308

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	1a02
Deposition date deposition_date	1997-12-08
Structure title title	STRUCTURE OF THE DNA BINDING DOMAINS OF NFAT, FOS AND JUN BOUND TO DNA
Keywords keywords	;TRANSCRIPTION FACTOR, NFAT, NF-AT, AP-1, FOS-JUN, QUATERNARY PROTEIN-DNA COMPLEX, TRANSCRIPTION SYNERGY, COMBINATORIAL GENE REGULATION, 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.

1a02__assembly_1__model_1

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

Download this curve (.dat)

1a02__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1a02__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	26.88 Å
Rg (electron density)	25.98 Å
Total Rg	26.76 Å
Atom count	3886
Residues	425
Excluded volume	66281 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1a02__assembly_1__model_1`	pentameric （5）	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 (6)

Entity 1 Entity 1 polymer

Description description	;DNA (5'-D(DTPDTPDGPDGPDAPDAPDAPDAPDTPDTPDTPDGPDTPDTPDTPDCPDAPDTPDAPDG)-3') ;
Molecular weight formula_weight	6178.0 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polydeoxyribonucleotide
Chain IDs strand_id	A
Atom count atom_count	3974

TTGGAAAATTTGTTTCATAG

Entity 2 Entity 2 polymer

Description description	;DNA (5'-D(DAPDAPDCPDTPDAPDTPDGPDAPDAPDAPDCPDAPDAPDAPDTPDTPDTPDTPDCPDC)-3') ;
Molecular weight formula_weight	6085.0 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polydeoxyribonucleotide
Chain IDs strand_id	B

AACTATGAAACAAATTTTCC

Entity 3 Entity 3 polymer

Description description	NUCLEAR FACTOR OF ACTIVATED T CELLS
Molecular weight formula_weight	34270.9 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	N

MRGSHHHHHHTDPHASSVPLEWPLSSQSGSYELRIEVQPKPHHRAHYETEGSRGAVKAPTGGHPVVQLHGYMENKPLGLQIFIGTADERILKPHAFYQVHRITGKTVTTTSYEKIVGNTKVLEIPLEPKNNMRATIDCAGILKLRNADIELRKGETDIGRKNTRVRLVFRVHIPESSGRIVSLQTASNPIECSQRSAHELPMVERQDTDSCLVYGGQQMILTGQNFTSESKVVFTEKTTDGQQIWEMEATVDKDKSQPNMLFVEIPEYRNKHIRTPVKVNFYVINGKRKRSQPQHFTYHPV

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 BL21(DE3)

Entity 4 Entity 4 polymer

Description description	AP-1 FRAGMENT FOS
Molecular weight formula_weight	6727.7 kDa
Mutation mutation	C154S
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	F

MKRRIRRERNKMAAAKSRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKL

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 5 Entity 5 polymer

Description description	AP-1 FRAGMENT JUN
Molecular weight formula_weight	6583.8 kDa
Mutation mutation	C279S
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	J

MKAERKRMRNRIAASKSRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQL

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 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	88

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6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1a02f_
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	d1a02j_
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	d1a02n1
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.18 — E set domains
Family Family family	b.1.18.1 — NF-kappa-B/REL/DORSAL transcription factors, C-terminal domain

Domain ID domain_id	d1a02n2
Class class	b — All beta proteins
Fold Fold fold	b.2 — Common fold of diphtheria toxin/transcription factors/cytochrome f
Superfamily Superfamily superfamily	b.2.5 — p53-like transcription factors
Family Family family	b.2.5.3 — Rel/Dorsal transcription factors, DNA-binding domain

CATH v4.4 (4 domains)

Domain ID domain_id	1a02F00
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	1a02J00
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	1a02N01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	340 — Rel homology domain (RHD), DNA-binding domain

Domain ID domain_id	1a02N02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

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Unit-cell length a length_a	64.660 Å
Unit-cell length b length_b	85.460 Å
Unit-cell length c length_c	83.370 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	112.03 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	2

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.700 Å
Low-resolution limit resolution_low	10.000 Å
R factor r_factor	0.2460
R_work r_work	0.2460
R_free r_free	0.3030

STRUCTURE OF THE DNA BINDING DOMAINS OF NFAT, FOS AND JUN BOUND TO DNA

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

NUCLEAR FACTOR OF ACTIVATED T CELLS

State in the Current Structure

Other States of the Same Protein in the Database

AP-1 FRAGMENT FOS

State in the Current Structure

Other States of the Same Protein in the Database

AP-1 FRAGMENT JUN

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

1a02__assembly_1__model_1

1a02__assembly_1__model_1 | I(q)

1a02__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 (6)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 polymer

Polymer Polymer

Source Source

Entity 5 Entity 5 polymer

Polymer Polymer

Source Source

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)

STRUCTURE OF THE DNA BINDING DOMAINS OF NFAT, FOS AND JUN BOUND TO DNA

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

NUCLEAR FACTOR OF ACTIVATED T CELLS

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

AP-1 FRAGMENT FOS

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

AP-1 FRAGMENT JUN

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

1a02__assembly_1__model_1

1a02__assembly_1__model_1 | I(q)

1a02__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 (6)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 polymer

Polymer Polymer

Source Source

Entity 5 Entity 5 polymer

Polymer Polymer

Source Source

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)