SAXSdb — 1tf3

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

TRANSCRIPTION FACTOR IIIA

Xenopus laevis

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–DNA	Monomer	Protein 1 DNA 2	5S RNA GENE × 1 5S RNA GENE × 1 ZINC ION × 3	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	TF3A_XENLA
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain A； PDBConstruct 1–92； UniProt 33–123

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	1tf3
Deposition date deposition_date	1997-07-01
Structure title title	TFIIIA FINGER 1-3 BOUND TO DNA, NMR, 22 STRUCTURES
Keywords keywords	;TFIIIA, PROTEIN, DNA, TRANSCRIPTION FACTOR, 5S RNA GENE, DNA BINDING PROTEIN, ZINC FINGER, COMPLEX (TRANSCRIPTION REGULATION-DNA), TRANSCRIPTION-DNA COMPLEX ;; TRANSCRIPTION/DNA
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.

1tf3__assembly_1__model_21

Assembly 1 · Model 21 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1tf3__assembly_1__model_21 | I(q)

100 plotted points; both axes use logarithmic scales.

1tf3__assembly_1__model_21 | P(r) · Pending

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

Rg（Guinier）	16.92 Å
Rg (electron density)	16.39 Å
Total Rg	17.19 Å
Atom count	2412
Residues	122
Excluded volume	22057 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1tf3__assembly_1__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	2	`1tf3__assembly_1__model_2`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	3	`1tf3__assembly_1__model_3`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	4	`1tf3__assembly_1__model_4`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	5	`1tf3__assembly_1__model_5`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	6	`1tf3__assembly_1__model_6`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	7	`1tf3__assembly_1__model_7`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	8	`1tf3__assembly_1__model_8`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	9	`1tf3__assembly_1__model_9`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	10	`1tf3__assembly_1__model_10`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	11	`1tf3__assembly_1__model_11`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	12	`1tf3__assembly_1__model_12`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	13	`1tf3__assembly_1__model_13`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	14	`1tf3__assembly_1__model_14`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	15	`1tf3__assembly_1__model_15`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	16	`1tf3__assembly_1__model_16`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	17	`1tf3__assembly_1__model_17`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	18	`1tf3__assembly_1__model_18`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	19	`1tf3__assembly_1__model_19`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	20	`1tf3__assembly_1__model_20`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	21	`1tf3__assembly_1__model_21`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	22	`1tf3__assembly_1__model_22`	trimeric （3）	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	5S RNA GENE
Molecular weight formula_weight	4690.0 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polydeoxyribonucleotide
Chain IDs strand_id	E
Atom count atom_count	53064

TTGGATGGGAGACCG

Entity 2 Entity 2 polymer

Description description	5S RNA GENE
Molecular weight formula_weight	4489.9 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polydeoxyribonucleotide
Chain IDs strand_id	F

CGGTCTCCCATCCAA

Entity 3 Entity 3 polymer

Description description	TRANSCRIPTION FACTOR IIIA
Molecular weight formula_weight	10686.2 kDa
Mutation mutation	C35S
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A

MKRYICSFADCGAAYNKNWKLQAHLSKHTGEKPFPCKEEGCEKGFTSLHHLTRHSLTHTGEKNFTCDSDGCDLRFTTKANMKKHFNRFHNIK

Source Source

Source organism organism	Xenopus laevis
Common name common_name	African clawed frog
NCBI taxonomy ID ncbi_taxonomy_id	8355
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 4 Entity 4 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	3

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1tf3a1
Class class	g — Small proteins
Fold Fold fold	g.37 — beta-beta-alpha zinc fingers
Superfamily Superfamily superfamily	g.37.1 — beta-beta-alpha zinc fingers
Family Family family	g.37.1.1 — Classic zinc finger, C2H2

Domain ID domain_id	d1tf3a2
Class class	g — Small proteins
Fold Fold fold	g.37 — beta-beta-alpha zinc fingers
Superfamily Superfamily superfamily	g.37.1 — beta-beta-alpha zinc fingers
Family Family family	g.37.1.1 — Classic zinc finger, C2H2

Domain ID domain_id	d1tf3a3
Class class	g — Small proteins
Fold Fold fold	g.37 — beta-beta-alpha zinc fingers
Superfamily Superfamily superfamily	g.37.1 — beta-beta-alpha zinc fingers
Family Family family	g.37.1.1 — Classic zinc finger, C2H2

CATH v4.4 (3 domains)

Domain ID domain_id	1tf3A01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	160 — Double Stranded RNA Binding Domain
Homologous superfamily homologous superfamily	60 — Classic Zinc Finger

Domain ID domain_id	1tf3A02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	160 — Double Stranded RNA Binding Domain
Homologous superfamily homologous superfamily	60 — Classic Zinc Finger

Domain ID domain_id	1tf3A03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	160 — Double Stranded RNA Binding Domain
Homologous superfamily homologous superfamily	60 — Classic Zinc Finger

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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	—

TFIIIA FINGER 1-3 BOUND TO DNA, NMR, 22 STRUCTURES

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

TRANSCRIPTION FACTOR IIIA

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

1tf3__assembly_1__model_21

1tf3__assembly_1__model_21 | I(q)

1tf3__assembly_1__model_21 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

5. Entities and Polymers Entities & Polymers (4)

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 non-polymer

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

7. Citations (2)

TFIIIA FINGER 1-3 BOUND TO DNA, NMR, 22 STRUCTURES

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

TRANSCRIPTION FACTOR IIIA

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

1tf3__assembly_1__model_21

1tf3__assembly_1__model_21 | I(q)

1tf3__assembly_1__model_21 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

5. Entities and Polymers Entities & Polymers (4)

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 non-polymer

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

7. Citations (2)