SAXSdb — 1iaz

▼

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

EQUINATOXIN II

Actinia equina

UniProt P61914

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	SULFATE ION × 11 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	EQT2_ACTEQ
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–179； UniProt 36–214 Author chain B； PDBConstruct 1–179； UniProt 36–214

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	1iaz
Deposition date deposition_date	2001-03-24
Structure title title	EQUINATOXIN II
Keywords keywords	beta-sandwich, TOXIN; TOXIN
Experimental Method method	X-RAY DIFFRACTION

▼

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.

1iaz__assembly_1__model_1

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

Download this curve (.dat)

1iaz__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1iaz__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	23.81 Å
Rg (electron density)	22.75 Å
Total Rg	23.51 Å
Atom count	2809
Residues	350
Excluded volume	49459 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1iaz__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	EQUINATOXIN II
Molecular weight formula_weight	19845.4 kDa
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	3186

SADVAGAVIDGASLSFDILKTVLEALGNVKRKIAVGVDNESGKTWTALNTYFRSGTSDIVLPHKVPHGKALLYNGQKDRGPVATGAVGVLAYLMSDGNTLAVLFSVPYDYNWYSNWWNVRIYKGKRRADQRMYEELYYNLSPFRGDNGWHTRNLGYGLKSRGFMNSSGHAILEIHVSKA

Source Source

Source organism organism	Actinia equina
NCBI taxonomy ID ncbi_taxonomy_id	6106
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	11

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	377

▼

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1iaza_
Class class	b — All beta proteins
Fold Fold fold	b.97 — Cytolysin/lectin
Superfamily Superfamily superfamily	b.97.1 — Cytolysin/lectin
Family Family family	b.97.1.1 — Anemone pore-forming cytolysin

Domain ID domain_id	d1iazb_
Class class	b — All beta proteins
Fold Fold fold	b.97 — Cytolysin/lectin
Superfamily Superfamily superfamily	b.97.1 — Cytolysin/lectin
Family Family family	b.97.1.1 — Anemone pore-forming cytolysin

CATH v4.4 (2 domains)

Domain ID domain_id	1iazA00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	270 — Mutm (Fpg) Protein; Chain: A, domain 2
Homologous superfamily homologous superfamily	20 — Cytolysin/lectin

Domain ID domain_id	1iazB00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	270 — Mutm (Fpg) Protein; Chain: A, domain 2
Homologous superfamily homologous superfamily	20 — Cytolysin/lectin

▶

Unit-cell length a length_a	81.620 Å
Unit-cell length b length_b	129.040 Å
Unit-cell length c length_c	31.760 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	8

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	12.000 Å
R factor r_factor	0.1900
R_work r_work	0.1850
R_free r_free	0.2350

EQUINATOXIN II

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

EQUINATOXIN II

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

1iaz__assembly_1__model_1

1iaz__assembly_1__model_1 | I(q)

1iaz__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

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)

EQUINATOXIN II

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

EQUINATOXIN II

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

1iaz__assembly_1__model_1

1iaz__assembly_1__model_1 | I(q)

1iaz__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

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)