SAXSdb — 1hi7

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

PS2 PROTEIN

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	PS2_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–60； UniProt 25–84 Author chain B； PDBConstruct 1–60； UniProt 25–84

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	1hi7
Deposition date deposition_date	2001-01-03
Structure title title	NMR SOLUTION STRUCTURE OF THE DISULPHIDE-LINKED HOMODIMER OF HUMAN TFF1, 10 STRUCTURES
Keywords keywords	GROWTH FACTOR, CELL MOTILITY, TUMOR SUPPRESSOR, TREFOIL DOMAIN; GROWTH FACTOR
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.

1hi7__assembly_1__model_7

Assembly 1 · Model 7 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1hi7__assembly_1__model_7 | I(q)

100 plotted points; both axes use logarithmic scales.

1hi7__assembly_1__model_7 | P(r) · Pending

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

Rg（Guinier）	27.04 Å
Rg (electron density)	27.20 Å
Total Rg	27.64 Å
Atom count	1752
Residues	120
Excluded volume	16090 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1hi7__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	2	`1hi7__assembly_1__model_2`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	3	`1hi7__assembly_1__model_3`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	4	`1hi7__assembly_1__model_4`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	5	`1hi7__assembly_1__model_5`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	6	`1hi7__assembly_1__model_6`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	7	`1hi7__assembly_1__model_7`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	8	`1hi7__assembly_1__model_8`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	9	`1hi7__assembly_1__model_9`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	10	`1hi7__assembly_1__model_10`	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	d1hi7a_
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	d1hi7b_
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	1hi7A00
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	1hi7B00
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	PS2 PROTEIN
Molecular weight formula_weight	6678.4 kDa
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	17520

Source organism organism	HOMO SAPIENS
Common name common_name	HUMAN
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	ESCHERICHIA COLI HB101

NMR SOLUTION STRUCTURE OF THE DISULPHIDE-LINKED HOMODIMER OF HUMAN TFF1, 10 STRUCTURES

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

PS2 PROTEIN

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

1hi7__assembly_1__model_7

1hi7__assembly_1__model_7 | I(q)

1hi7__assembly_1__model_7 | 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 (5)

NMR SOLUTION STRUCTURE OF THE DISULPHIDE-LINKED HOMODIMER OF HUMAN TFF1, 10 STRUCTURES

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

PS2 PROTEIN

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

1hi7__assembly_1__model_7

1hi7__assembly_1__model_7 | I(q)

1hi7__assembly_1__model_7 | 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 (5)