SAXSdb — 1iqb

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

AGGLUTININ ISOLECTIN I

OrganismNot specified

State in the Current Structure

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

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	AGI_URTDI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–89； UniProt 25–112 Author chain B； PDBConstruct 1–89； UniProt 25–112

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	1iqb
Deposition date deposition_date	2001-07-15
Structure title title	Crystal Structure of Urtica dioica Agglutinin Isolectin I
Keywords keywords	TWO HOMOLOGOUS HEVEIN-LIKE DOMAINS, ZINC COMPLEX, HOMO-DIMER, SUGAR BINDING PROTEIN; SUGAR BINDING 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.

1iqb__assembly_1__model_1

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

Download this curve (.dat)

1iqb__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1iqb__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	19.87 Å
Rg (electron density)	20.08 Å
Total Rg	20.43 Å
Atom count	1294
Residues	176
Excluded volume	21876 Å³
Maximum q	0.500 Å⁻¹

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

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1iqba1
Class class	g — Small proteins
Fold Fold fold	g.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamily	g.3.1 — Plant lectins/antimicrobial peptides
Family Family family	g.3.1.1 — Hevein-like agglutinin (lectin) domain

Domain ID domain_id	d1iqba2
Class class	g — Small proteins
Fold Fold fold	g.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamily	g.3.1 — Plant lectins/antimicrobial peptides
Family Family family	g.3.1.1 — Hevein-like agglutinin (lectin) domain

Domain ID domain_id	d1iqbb1
Class class	g — Small proteins
Fold Fold fold	g.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamily	g.3.1 — Plant lectins/antimicrobial peptides
Family Family family	g.3.1.1 — Hevein-like agglutinin (lectin) domain

Domain ID domain_id	d1iqbb2
Class class	g — Small proteins
Fold Fold fold	g.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamily	g.3.1 — Plant lectins/antimicrobial peptides
Family Family family	g.3.1.1 — Hevein-like agglutinin (lectin) domain

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Unit-cell length a length_a	30.710 Å
Unit-cell length b length_b	42.110 Å
Unit-cell length c length_c	62.590 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	101.55 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	—
R_work r_work	0.2050
R_free r_free	0.2600

Description description	AGGLUTININ ISOLECTIN I
Molecular weight formula_weight	9408.4 kDa
Mutation mutation	Q1(PCA)
Source method src_method	nat
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	1381

Crystal Structure of Urtica dioica Agglutinin Isolectin I

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

AGGLUTININ ISOLECTIN I

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

1iqb__assembly_1__model_1

1iqb__assembly_1__model_1 | I(q)

1iqb__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

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (4 domains)

7. Citations (1)

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	2

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	87

Crystal Structure of Urtica dioica Agglutinin Isolectin I

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

AGGLUTININ ISOLECTIN I

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

1iqb__assembly_1__model_1

1iqb__assembly_1__model_1 | I(q)

1iqb__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

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (4 domains)

7. Citations (1)