SAXSdb — 1bwu

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

PROTEIN (AGGLUTININ)

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	PROTEIN (AGGLUTININ) × 1 （Q38784） PROTEIN (AGGLUTININ) × 1 （Q38784） alpha-D-mannopyranose × 14 water × 4	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	PROTEIN (AGGLUTININ) × 1 （Q38784） alpha-D-mannopyranose × 7 water × 2	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	PROTEIN (AGGLUTININ) × 1 （Q38784） alpha-D-mannopyranose × 7 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q38789_ALLSA
Isoform	—
PDB entities	1, 3
Chains and sequence ranges	Author chain A； PDBConstruct 1–106； UniProt 177–282 Author chain P； PDBConstruct 1–106； UniProt 18–123

PROTEIN (AGGLUTININ)

OrganismNot specified

UniProt Q38784

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	PROTEIN (AGGLUTININ) × 1 （Q38789） PROTEIN (AGGLUTININ) × 1 （Q38789） alpha-D-mannopyranose × 14 water × 4	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	PROTEIN (AGGLUTININ) × 1 （Q38789） alpha-D-mannopyranose × 7 water × 2	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	PROTEIN (AGGLUTININ) × 1 （Q38789） alpha-D-mannopyranose × 7 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q38784_ALLSA
Isoform	—
PDB entities	2, 4
Chains and sequence ranges	Author chain D； PDBConstruct 1–109； UniProt 25–133 Author chain Q； PDBConstruct 1–109； UniProt 25–133

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	1bwu
Deposition date deposition_date	1998-09-28
Structure title title	MANNOSE-SPECIFIC AGGLUTININ (LECTIN) FROM GARLIC (ALLIUM SATIVUM) BULBS COMPLEXED WITH ALPHA-D-MANNOSE
Keywords keywords	BULB LECTIN, MANNOSE, PLANT PROTEIN; PLANT PROTEIN
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.

1bwu__assembly_1__model_1

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

Download this curve (.dat)

1bwu__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1bwu__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	27.29 Å
Rg (electron density)	26.48 Å
Total Rg	27.26 Å
Atom count	3527
Residues	430
Excluded volume	61675 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1bwu__assembly_1__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1bwu__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`1bwu__assembly_3__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 (6)

Entity 1 Entity 1 polymer

Description description	PROTEIN (AGGLUTININ)
Molecular weight formula_weight	11865.1 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	3664

RNILRNDEGLYGGQSLDVNPYHFIMQEDCNLVLYDHSTSVWASNTGILGKKGCRAVLQSDGNFVVYDAEGRSLWASHSVRGNGNYVLVLQEDGNVVIYRSDIWSTN

Entity 2 Entity 2 polymer

Description description	PROTEIN (AGGLUTININ)
Molecular weight formula_weight	12124.3 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D

RNILTNDEGLYGGQSLDVNPYHLIMQEDCNLVLYDHSTAVWSSNTDIPGKKGCKAVLQSDGNFVVYDAEGASLWASHSVRGNGNYVLVLQEDGNVVIYRSDIWSTNTYR

Entity 3 Entity 3 polymer

Description description	PROTEIN (AGGLUTININ)
Molecular weight formula_weight	11678.9 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	P

RNILTNDEGLYAGQSLDVNPYHFIMQEDCNLVLYDHSTSVWASNTGILGKKGCKAVLQADGNFVVYDAEGRSLWASHSVRGNGNYVLVLQEDGNVVIYGSDIWSTN

Entity 4 Entity 4 polymer

Description description	PROTEIN (AGGLUTININ)
Molecular weight formula_weight	12010.2 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	Q

RNILTNDEGLYAGQSLDVNPYHLIMQEDCNLVLYDHSTAVWSSNTDIPGKKGCKAVLQSDGNFVVYDAEGASLWASHSVRGNGNYVLVLQEDGNVVIYGSDIWSTNTYK

Entity 5 Entity 5 non-polymer

Description description	alpha-D-mannopyranose
Molecular weight formula_weight	180.2 kDa
Source method src_method	syn
Copy count entity_count	14

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	137

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6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1bwua_
Class class	b — All beta proteins
Fold Fold fold	b.78 — beta-Prism II
Superfamily Superfamily superfamily	b.78.1 — alpha-D-mannose-specific plant lectins
Family Family family	b.78.1.1 — alpha-D-mannose-specific plant lectins

Domain ID domain_id	d1bwud_
Class class	b — All beta proteins
Fold Fold fold	b.78 — beta-Prism II
Superfamily Superfamily superfamily	b.78.1 — alpha-D-mannose-specific plant lectins
Family Family family	b.78.1.1 — alpha-D-mannose-specific plant lectins

Domain ID domain_id	d1bwup_
Class class	b — All beta proteins
Fold Fold fold	b.78 — beta-Prism II
Superfamily Superfamily superfamily	b.78.1 — alpha-D-mannose-specific plant lectins
Family Family family	b.78.1.1 — alpha-D-mannose-specific plant lectins

Domain ID domain_id	d1bwuq_
Class class	b — All beta proteins
Fold Fold fold	b.78 — beta-Prism II
Superfamily Superfamily superfamily	b.78.1 — alpha-D-mannose-specific plant lectins
Family Family family	b.78.1.1 — alpha-D-mannose-specific plant lectins

CATH v4.4 (4 domains)

Domain ID domain_id	1bwuA00
Class class	2 — Mainly Beta
Architecture architecture	90 — Orthogonal Prism
Topology topology	10 — Agglutinin, subunit A
Homologous superfamily homologous superfamily	10 — Bulb-type lectin domain

Domain ID domain_id	1bwuD00
Class class	2 — Mainly Beta
Architecture architecture	90 — Orthogonal Prism
Topology topology	10 — Agglutinin, subunit A
Homologous superfamily homologous superfamily	10 — Bulb-type lectin domain

Domain ID domain_id	1bwuP00
Class class	2 — Mainly Beta
Architecture architecture	90 — Orthogonal Prism
Topology topology	10 — Agglutinin, subunit A
Homologous superfamily homologous superfamily	10 — Bulb-type lectin domain

Domain ID domain_id	1bwuQ00
Class class	2 — Mainly Beta
Architecture architecture	90 — Orthogonal Prism
Topology topology	10 — Agglutinin, subunit A
Homologous superfamily homologous superfamily	10 — Bulb-type lectin domain

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Unit-cell length a length_a	203.243 Å
Unit-cell length b length_b	43.780 Å
Unit-cell length c length_c	79.268 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	112.37 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

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

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	9.000 Å
R factor r_factor	0.2260
R_work r_work	0.2260
R_free r_free	0.2780

MANNOSE-SPECIFIC AGGLUTININ (LECTIN) FROM GARLIC (ALLIUM SATIVUM) BULBS COMPLEXED WITH ALPHA-D-MANNOSE

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

PROTEIN (AGGLUTININ)

State in the Current Structure

Other States of the Same Protein in the Database

PROTEIN (AGGLUTININ)

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

1bwu__assembly_1__model_1

1bwu__assembly_1__model_1 | I(q)

1bwu__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 (6)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (2)

MANNOSE-SPECIFIC AGGLUTININ (LECTIN) FROM GARLIC (ALLIUM SATIVUM) BULBS COMPLEXED WITH ALPHA-D-MANNOSE

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

PROTEIN (AGGLUTININ)

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

PROTEIN (AGGLUTININ)

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

1bwu__assembly_1__model_1

1bwu__assembly_1__model_1 | I(q)

1bwu__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 (6)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (2)