SAXSdb — 3g4o

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

Aerolysin

Aeromonas hydrophila

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	AERA_AERHY
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–470； UniProt 24–493 Author chain B； PDBConstruct 1–470； UniProt 24–493

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	3g4o
Deposition date deposition_date	2009-02-04
Structure title title	Crystal structure of the activated aerolysin mutant H132N
Keywords keywords	TOXIN, CYTOLYTIC TOXIN, PORE-FORMING TOXIN, Membrane, Secreted; 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.

3g4o__assembly_1__model_1

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

Download this curve (.dat)

3g4o__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3g4o__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	33.04 Å
Rg (electron density)	32.52 Å
Total Rg	32.96 Å
Atom count	6978
Residues	890
Excluded volume	122560 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3g4o__assembly_1__model_1`	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 (2)

Entity 1 Entity 1 polymer

Description description	Aerolysin
Molecular weight formula_weight	51956.4 kDa
Mutation mutation	H132N
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	7165

AEPVYPDQLRLFSLGQGVCGDKYRPVNREEAQSVKSNIVGMMGQWQISGLANGWVIMGPGYNGEIKPGTASNTWCYPTNPVTGEIPTLSALDIPDGDEVDVQWRLVHDSANFIKPTSYLAHYLGYAWVGGNNSQYVGEDMDVTRDGDGWVIRGNNDGGCDGYRCGDKTAIKVSNFAYNLDPDSFKHGDVTQSDRQLVKTVVGWAVNDSDTPQSGYDVTLRYDTATNWSKTNTYGLSEKVTTKNKFKWPLVGETELSIEIAANQSWASQNGGSTTTSLSQSVRPTVPARSKIPVKIELYKADISYPYEFKADVSYDLTLSGFLRWGGNAWYTHPDNRPNWNHTFVIGPYKDKASSIRYQWDKRYIPGEVKWWDWNWTIQQNGLSTMQNNLARVLRPVRAGITGDFSAESQFAGNIEIGAPVPLAADSKVRRARSVDGAGQGLRLEIPLDAQELSGLGFNNVSLSVTPAANQ

Source Source

Source organism organism	Aeromonas hydrophila
NCBI taxonomy ID ncbi_taxonomy_id	644
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	187

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6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d3g4oa1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.169 — C-type lectin-like
Superfamily Superfamily superfamily	d.169.1 — C-type lectin-like
Family Family family	d.169.1.2 — Aerolysin/Pertussis toxin (APT) domain

Domain ID domain_id	d3g4oa2
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.8.1.1 — (Pro)aerolysin, pore-forming lobe

Domain ID domain_id	d3g4ob1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.169 — C-type lectin-like
Superfamily Superfamily superfamily	d.169.1 — C-type lectin-like
Family Family family	d.169.1.2 — Aerolysin/Pertussis toxin (APT) domain

Domain ID domain_id	d3g4ob2
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.8.1.1 — (Pro)aerolysin, pore-forming lobe

CATH v4.4 (6 domains)

Domain ID domain_id	3g4oA01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	40 — Pertussis Toxin; Chain B, domain 1
Homologous superfamily homologous superfamily	10 — Aerolysin/Pertussis toxin (APT), N-terminal domain

Domain ID domain_id	3g4oA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	412 — Proaerolysin; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — Proaerolysin, chain A, domain 2

Domain ID domain_id	3g4oA03
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	3g4oB01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	40 — Pertussis Toxin; Chain B, domain 1
Homologous superfamily homologous superfamily	10 — Aerolysin/Pertussis toxin (APT), N-terminal domain

Domain ID domain_id	3g4oB02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	412 — Proaerolysin; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — Proaerolysin, chain A, domain 2

Domain ID domain_id	3g4oB03
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	95.985 Å
Unit-cell length b length_b	69.313 Å
Unit-cell length c length_c	165.230 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	109.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	55.470 Å
R factor r_factor	0.2079
R_work r_work	0.2050
R_free r_free	0.2597

Crystal structure of the activated aerolysin mutant H132N

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

Aerolysin

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

3g4o__assembly_1__model_1

3g4o__assembly_1__model_1 | I(q)

3g4o__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

CATH v4.4 (6 domains)

7. Citations (2)

Crystal structure of the activated aerolysin mutant H132N

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

Aerolysin

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

3g4o__assembly_1__model_1

3g4o__assembly_1__model_1 | I(q)

3g4o__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

CATH v4.4 (6 domains)

7. Citations (2)