SAXSdb — 1uyj

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

EPSILON-TOXIN

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 3	URANIUM ATOM × 9 water × 3	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 3	URANIUM ATOM × 15 water × 3	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 3	URANIUM ATOM × 12 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q57398
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–296； UniProt 33–328 Author chain B； PDBConstruct 1–296； UniProt 33–328 Author chain C； PDBConstruct 1–296； UniProt 33–328

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	1uyj
Deposition date deposition_date	2004-03-02
Structure title title	Clostridium perfringens epsilon toxin shows structural similarity with the pore forming toxin aerolysin
Keywords keywords	TOXIN, BETA PORE FORMING TOXIN; TOXIN
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.

1uyj__assembly_1__model_1

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

Download this curve (.dat)

1uyj__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1uyj__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	38.43 Å
Rg (electron density)	38.44 Å
Total Rg	37.93 Å
Atom count	6225
Residues	819
Excluded volume	110090 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1uyj__assembly_1__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1uyj__assembly_2__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`1uyj__assembly_3__model_1`	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 (3)

Entity 1 Entity 1 polymer

Description description	EPSILON-TOXIN
Molecular weight formula_weight	33015.8 kDa
Source method src_method	nat
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	6320

KEISNTVSNEMSKKASYDNVDTLIEKGRYNTKYNYLKRMEKYYPNAMAYFDKVTINPQGNDFYINNPKVELDGEPSMNYLEDVYVGKALLTNDTQQEQKLKSQSFTCKNTDTVTATTTHTVGTSIQATAKFTVPFNETGVSLTTSYSFANTNTNTNSKEITHNVPSQDILVPANTTVEVIAYLKKVNVKGNVKLVGQVSGSEWGEIPSYLAFPRDGYKFSLSDTVNKSDLNEDGTININGKGNYSAVMGDELIVKVRNLNTNNVQEYVIPVDKKEKSNDSNIVKYRSLSIKAPGIK

Entity 2 Entity 2 non-polymer

Description description	URANIUM ATOM
Molecular weight formula_weight	238.0 kDa
Source method src_method	syn
Copy count entity_count	12

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	52

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6. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1uyja_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.8 — Aerolisin/ETX pore-forming domain
Superfamily Superfamily superfamily	f.8.1 — Aerolisin/ETX pore-forming domain
Family Family family	f.8.1.2 — ETX/MTX2

Domain ID domain_id	d1uyjb_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.8 — Aerolisin/ETX pore-forming domain
Superfamily Superfamily superfamily	f.8.1 — Aerolisin/ETX pore-forming domain
Family Family family	f.8.1.2 — ETX/MTX2

Domain ID domain_id	d1uyjc_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.8 — Aerolisin/ETX pore-forming domain
Superfamily Superfamily superfamily	f.8.1 — Aerolisin/ETX pore-forming domain
Family Family family	f.8.1.2 — ETX/MTX2

CATH v4.4 (6 domains)

Domain ID domain_id	1uyjA01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	360 — Dihydrodipicolinate Reductase; domain 2
Homologous superfamily homologous superfamily	60 —

Domain ID domain_id	1uyjA02
Class class	2 — Mainly Beta
Architecture architecture	170 — Beta Complex
Topology topology	15 — Proaerolysin; Chain A, domain 3
Homologous superfamily homologous superfamily	10 — Proaerolysin, chain A, domain 3

Domain ID domain_id	1uyjB01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	360 — Dihydrodipicolinate Reductase; domain 2
Homologous superfamily homologous superfamily	60 —

Domain ID domain_id	1uyjB02
Class class	2 — Mainly Beta
Architecture architecture	170 — Beta Complex
Topology topology	15 — Proaerolysin; Chain A, domain 3
Homologous superfamily homologous superfamily	10 — Proaerolysin, chain A, domain 3

Domain ID domain_id	1uyjC01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	360 — Dihydrodipicolinate Reductase; domain 2
Homologous superfamily homologous superfamily	60 —

Domain ID domain_id	1uyjC02
Class class	2 — Mainly Beta
Architecture architecture	170 — Beta Complex
Topology topology	15 — Proaerolysin; Chain A, domain 3
Homologous superfamily homologous superfamily	10 — Proaerolysin, chain A, domain 3

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Unit-cell length a length_a	125.962 Å
Unit-cell length b length_b	125.962 Å
Unit-cell length c length_c	121.862 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	18

Space group space_group	P 63
Space-group number int_tables_number	173
Crystal system crystal_system	—

Resolution resolution	2.600 Å
Low-resolution limit resolution_low	50.000 Å
R factor r_factor	0.2391
R_work r_work	0.2363
R_free r_free	0.2901

Clostridium perfringens epsilon toxin shows structural similarity with the pore forming toxin aerolysin

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

EPSILON-TOXIN

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

1uyj__assembly_1__model_1

1uyj__assembly_1__model_1 | I(q)

1uyj__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (3 domains)

CATH v4.4 (6 domains)

7. Citations (1)

Clostridium perfringens epsilon toxin shows structural similarity with the pore forming toxin aerolysin

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

EPSILON-TOXIN

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

1uyj__assembly_1__model_1

1uyj__assembly_1__model_1 | I(q)

1uyj__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (3 domains)

CATH v4.4 (6 domains)

7. Citations (1)