SAXSdb — 1w3a

▼

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

HEMOLYTIC LECTIN LSLA

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Other combination	Homooligomer	Protein 6 其他Polymer 6	beta-D-galactopyranose-(1-4)-alpha-D-glucopyranose × 6 GLYCEROL × 36 water × 6	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q7Z8V1_9APHY
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–315； UniProt 1–315

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	1w3a
Deposition date deposition_date	2004-07-14
Structure title title	Three dimensional structure of a novel pore-forming lectin from the mushroom Laetiporus sulphureus
Keywords keywords	TOXIN, PORE-FORMING TOXIN, HEMOLYTIC LECTIN, OLIGOMER, BETA-TREFOIL, SUGAR-BINDING PROTEIN, TOXIN-SUGAR BINDING PROTEIN complex; TOXIN/SUGAR BINDING PROTEIN
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.

1w3a__assembly_1__model_1

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

Download this curve (.dat)

1w3a__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1w3a__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	50.99 Å
Rg (electron density)	51.40 Å
Total Rg	51.16 Å
Atom count	15156
Residues	1878
Excluded volume	268890 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1w3a__assembly_1__model_1`	hexameric （6）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	HEMOLYTIC LECTIN LSLA
Molecular weight formula_weight	35125.0 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2603

MTDIYIPPEGLYFRLLGFASRQVIFARNSPSPDVGLSPVNDQATDQYFSLIYGTGEHAGLYAIKSKATGKVLFSRRPAEPYVGQIDGDGRYPDNWFKIEPGKTYLSKYFRLVQPSTGTALVSRTHLQPYFWNHPQTEVFDDQYFTFLFEDMSIDKIEYDLKDGRILSSTPNVLATQTLENTSSQTQEMSFNLSQTLTQTSTFAYTAGFTIAVGTAFKAGVPIFAETEFKVDISVDNQWNWGEENTFSKTYTATFSVRAGPGETVKAVSTVDSGIINVPFTAYLSSKSTGFEVTTEGIWRGVSSWDLRHTLTSVTA

Entity 2 Entity 2 branched

Description description	beta-D-galactopyranose-(1-4)-alpha-D-glucopyranose
Molecular weight formula_weight	342.3 kDa
Source method src_method	man
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	77

▼

6. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id	1w3aA01
Class class	2 — Mainly Beta
Architecture architecture	80 — Trefoil
Topology topology	10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily	50 —

Domain ID domain_id	1w3aA02
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

▶

Unit-cell length a length_a	101.526 Å
Unit-cell length b length_b	101.526 Å
Unit-cell length c length_c	193.435 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	12

Space group space_group	P 63 2 2
Space-group number int_tables_number	182
Crystal system crystal_system	—

Resolution resolution	2.650 Å
Low-resolution limit resolution_low	14.990 Å
R factor r_factor	0.2290
R_work r_work	0.2260
R_free r_free	0.2800

Three dimensional structure of a novel pore-forming lectin from the mushroom Laetiporus sulphureus

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

HEMOLYTIC LECTIN LSLA

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

1w3a__assembly_1__model_1

1w3a__assembly_1__model_1 | I(q)

1w3a__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 branched

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

7. Citations (1)

Three dimensional structure of a novel pore-forming lectin from the mushroom Laetiporus sulphureus

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

HEMOLYTIC LECTIN LSLA

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

1w3a__assembly_1__model_1

1w3a__assembly_1__model_1 | I(q)

1w3a__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 branched

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

7. Citations (1)