SAXSdb — 9uj0

▼

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

Aeg-L

Alternaria alternata

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 36	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0AB39ISW4_ALTAL
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–203； UniProt 1–203 Author chain A； PDBConstruct 212–488； UniProt 214–490 Author chain B； PDBConstruct 1–203； UniProt 1–203 Author chain B； PDBConstruct 212–488； UniProt 214–490 Author chain C； PDBConstruct 1–203； UniProt 1–203 Author chain C； PDBConstruct 212–488； UniProt 214–490 Author chain D； PDBConstruct 1–203； UniProt 1–203 Author chain D； PDBConstruct 212–488； UniProt 214–490 Author chain E； PDBConstruct 1–203； UniProt 1–203 Author chain E； PDBConstruct 212–488； UniProt 214–490 Author chain F； PDBConstruct 1–203； UniProt 1–203 Author chain F； PDBConstruct 212–488； UniProt 214–490 Author chain G； PDBConstruct 1–203； UniProt 1–203 Author chain G； PDBConstruct 212–488； UniProt 214–490 Author chain H； PDBConstruct 1–203； UniProt 1–203 Author chain H； PDBConstruct 212–488； UniProt 214–490 Author chain I； PDBConstruct 1–203； UniProt 1–203 Author chain I； PDBConstruct 212–488； UniProt 214–490 Author chain J； PDBConstruct 1–203； UniProt 1–203 Author chain J； PDBConstruct 212–488； UniProt 214–490 Author chain K； PDBConstruct 1–203； UniProt 1–203 Author chain K； PDBConstruct 212–488； UniProt 214–490 Author chain L； PDBConstruct 1–203； UniProt 1–203 Author chain L； PDBConstruct 212–488； UniProt 214–490 Author chain M； PDBConstruct 1–203； UniProt 1–203 Author chain M； PDBConstruct 212–488； UniProt 214–490 Author chain N； PDBConstruct 1–203； UniProt 1–203 Author chain N； PDBConstruct 212–488； UniProt 214–490 Author chain O； PDBConstruct 1–203； UniProt 1–203 Author chain O； PDBConstruct 212–488； UniProt 214–490 Author chain P； PDBConstruct 1–203； UniProt 1–203 Author chain P； PDBConstruct 212–488； UniProt 214–490 Author chain Q； PDBConstruct 1–203； UniProt 1–203 Author chain Q； PDBConstruct 212–488； UniProt 214–490 Author chain R； PDBConstruct 1–203； UniProt 1–203 Author chain R； PDBConstruct 212–488； UniProt 214–490 Author chain a； PDBConstruct 1–203； UniProt 1–203 Author chain a； PDBConstruct 212–488； UniProt 214–490 Author chain b； PDBConstruct 1–203； UniProt 1–203 Author chain b； PDBConstruct 212–488； UniProt 214–490 Author chain c； PDBConstruct 1–203； UniProt 1–203 Author chain c； PDBConstruct 212–488； UniProt 214–490 Author chain d； PDBConstruct 1–203； UniProt 1–203 Author chain d； PDBConstruct 212–488； UniProt 214–490 Author chain e； PDBConstruct 1–203； UniProt 1–203 Author chain e； PDBConstruct 212–488； UniProt 214–490 Author chain f； PDBConstruct 1–203； UniProt 1–203 Author chain f； PDBConstruct 212–488； UniProt 214–490 Author chain g； PDBConstruct 1–203； UniProt 1–203 Author chain g； PDBConstruct 212–488； UniProt 214–490 Author chain h； PDBConstruct 1–203； UniProt 1–203 Author chain h； PDBConstruct 212–488； UniProt 214–490 Author chain i； PDBConstruct 1–203； UniProt 1–203 Author chain i； PDBConstruct 212–488； UniProt 214–490 Author chain j； PDBConstruct 1–203； UniProt 1–203 Author chain j； PDBConstruct 212–488； UniProt 214–490 Author chain k； PDBConstruct 1–203； UniProt 1–203 Author chain k； PDBConstruct 212–488； UniProt 214–490 Author chain l； PDBConstruct 1–203； UniProt 1–203 Author chain l； PDBConstruct 212–488； UniProt 214–490 Author chain m； PDBConstruct 1–203； UniProt 1–203 Author chain m； PDBConstruct 212–488； UniProt 214–490 Author chain n； PDBConstruct 1–203； UniProt 1–203 Author chain n； PDBConstruct 212–488； UniProt 214–490 Author chain o； PDBConstruct 1–203； UniProt 1–203 Author chain o； PDBConstruct 212–488； UniProt 214–490 Author chain p； PDBConstruct 1–203； UniProt 1–203 Author chain p； PDBConstruct 212–488； UniProt 214–490 Author chain q； PDBConstruct 1–203； UniProt 1–203 Author chain q； PDBConstruct 212–488； UniProt 214–490 Author chain r； PDBConstruct 1–203； UniProt 1–203 Author chain r； PDBConstruct 212–488； UniProt 214–490

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	9uj0
Deposition date deposition_date	2025-04-16
Structure title title	Structure of Aegerolysin-L pore
Keywords keywords	Alternaria alternata pore-forming toxin, Aeg-L, TOXIN; TOXIN
Experimental Method method	ELECTRON MICROSCOPY

▼

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.

9uj0__assembly_1__model_1

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

Download this curve (.dat)

9uj0__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

9uj0__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	97.26 Å
Rg (electron density)	95.92 Å
Total Rg	96.09 Å
Atom count	130464
Residues	16164
Excluded volume	2317300 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`9uj0__assembly_1__model_1`	36-meric （36）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (1)

▶

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	—

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	3.81 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	494713

Description description	Aeg-L
Molecular weight formula_weight	55447.2 kDa
Source method src_method	man
Copy count entity_count	36

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,a,b,c,d,e,f,g,h,i,j,k,l,m,n,o,p,q,r
Atom count atom_count	130464

Structure of Aegerolysin-L pore

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

Aeg-L

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

9uj0__assembly_1__model_1

9uj0__assembly_1__model_1 | I(q)

9uj0__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

7. Citations (1)

Source organism organism	Alternaria alternata
NCBI taxonomy ID ncbi_taxonomy_id	5599
Host organism host_organism	Escherichia coli

Structure of Aegerolysin-L pore

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

Aeg-L

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

9uj0__assembly_1__model_1

9uj0__assembly_1__model_1 | I(q)

9uj0__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

7. Citations (1)