1pe3

Solution structure of the disulphide-linked dimer of human intestinal trefoil factor (TFF3)

Method: SOLUTION NMR

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

Trefoil factor 3

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	TFF3_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain 1； PDBConstruct 1–59； UniProt 22–80 Author chain 2； PDBConstruct 1–59； UniProt 22–80

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	1pe3
Deposition date deposition_date	2003-05-21
Structure title title	Solution structure of the disulphide-linked dimer of human intestinal trefoil factor (TFF3)
Keywords keywords	;intestinal trefoil factor, ITF, trefoil factor family, TFF3, TFF3 dimer, trefoil motif, solution structure, NMR spectroscopy, CELL CYCLE ;; CELL CYCLE
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.

1pe3__assembly_1__model_8

Assembly 1 · Model 8 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1pe3__assembly_1__model_8 | I(q)

100 plotted points; both axes use logarithmic scales.

1pe3__assembly_1__model_8 | P(r) · Pending

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

Rg（Guinier）	15.10 Å
Rg (electron density)	14.70 Å
Total Rg	15.55 Å
Atom count	1756
Residues	118
Excluded volume	16026 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1pe3__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	2	`1pe3__assembly_1__model_2`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	3	`1pe3__assembly_1__model_3`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	4	`1pe3__assembly_1__model_4`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	5	`1pe3__assembly_1__model_5`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	6	`1pe3__assembly_1__model_6`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	7	`1pe3__assembly_1__model_7`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	8	`1pe3__assembly_1__model_8`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	9	`1pe3__assembly_1__model_9`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	10	`1pe3__assembly_1__model_10`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	11	`1pe3__assembly_1__model_11`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	12	`1pe3__assembly_1__model_12`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	13	`1pe3__assembly_1__model_13`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	14	`1pe3__assembly_1__model_14`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	15	`1pe3__assembly_1__model_15`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	16	`1pe3__assembly_1__model_16`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	17	`1pe3__assembly_1__model_17`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	18	`1pe3__assembly_1__model_18`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	19	`1pe3__assembly_1__model_19`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	20	`1pe3__assembly_1__model_20`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	21	`1pe3__assembly_1__model_21`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	22	`1pe3__assembly_1__model_22`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	23	`1pe3__assembly_1__model_23`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	24	`1pe3__assembly_1__model_24`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	25	`1pe3__assembly_1__model_25`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	26	`1pe3__assembly_1__model_26`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	27	`1pe3__assembly_1__model_27`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	28	`1pe3__assembly_1__model_28`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	29	`1pe3__assembly_1__model_29`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	30	`1pe3__assembly_1__model_30`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	31	`1pe3__assembly_1__model_31`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	32	`1pe3__assembly_1__model_32`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	33	`1pe3__assembly_1__model_33`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	34	`1pe3__assembly_1__model_34`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	35	`1pe3__assembly_1__model_35`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	36	`1pe3__assembly_1__model_36`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	37	`1pe3__assembly_1__model_37`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	38	`1pe3__assembly_1__model_38`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	39	`1pe3__assembly_1__model_39`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	40	`1pe3__assembly_1__model_40`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	41	`1pe3__assembly_1__model_41`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	42	`1pe3__assembly_1__model_42`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	43	`1pe3__assembly_1__model_43`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	44	`1pe3__assembly_1__model_44`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	45	`1pe3__assembly_1__model_45`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	46	`1pe3__assembly_1__model_46`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	47	`1pe3__assembly_1__model_47`	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	d1pe31_
Class class	g — Small proteins
Fold Fold fold	g.16 — Trefoil/Plexin domain-like
Superfamily Superfamily superfamily	g.16.1 — Trefoil
Family Family family	g.16.1.1 — Trefoil

Domain ID domain_id	d1pe32_
Class class	g — Small proteins
Fold Fold fold	g.16 — Trefoil/Plexin domain-like
Superfamily Superfamily superfamily	g.16.1 — Trefoil
Family Family family	g.16.1.1 — Trefoil

CATH v4.4 (2 domains)

Domain ID domain_id	1pe3100
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	110 — Spasmolytic Protein; domain 1
Homologous superfamily homologous superfamily	10 — Spasmolytic Protein, domain 1

Domain ID domain_id	1pe3200
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	110 — Spasmolytic Protein; domain 1
Homologous superfamily homologous superfamily	10 — Spasmolytic Protein, domain 1

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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	Trefoil factor 3
Molecular weight formula_weight	6587.5 kDa
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	1,2
Atom count atom_count	82532

Source organism organism	Homo sapiens
Common name common_name	human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli BL21

Solution structure of the disulphide-linked dimer of human intestinal trefoil factor (TFF3)

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

Trefoil factor 3

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

1pe3__assembly_1__model_8

1pe3__assembly_1__model_8 | I(q)

1pe3__assembly_1__model_8 | 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 (1)

Solution structure of the disulphide-linked dimer of human intestinal trefoil factor (TFF3)

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

Trefoil factor 3

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

1pe3__assembly_1__model_8

1pe3__assembly_1__model_8 | I(q)

1pe3__assembly_1__model_8 | 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 (1)