SAXSdb — 1ouw

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

lectin

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	1,2-ETHANEDIOL × 5 IMIDAZOLE × 4 water × 2	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	1,2-ETHANEDIOL × 4 D-MALATE × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	P93114_CALSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–152； UniProt 2–153 Author chain B； PDBConstruct 1–152； UniProt 2–153 Author chain C； PDBConstruct 1–152； UniProt 2–153 Author chain D； PDBConstruct 1–152； UniProt 2–153

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	1ouw
Deposition date deposition_date	2003-03-25
Structure title title	Crystal structure of Calystegia sepium agglutinin
Keywords keywords	beta-prism fold, agglutinin, lectin, mannose-binding, jacalin-related, 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.

1ouw__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1ouw__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1ouw__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	20.21 Å
Rg (electron density)	19.11 Å
Total Rg	20.01 Å
Atom count	2264
Residues	301
Excluded volume	39775 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1ouw__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1ouw__assembly_2__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 (5)

Entity 1 Entity 1 polymer

Description description	lectin
Molecular weight formula_weight	15985.6 kDa
Source method src_method	nat
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	5125

AVPMDTISGPWGNNGGNFWSFRPVNKINQIVISYGGGGNNPIALTFSSTKADGSKDTITVGGGGPDSITGTEMVNIGTDEYLTGISGTFGIYLDNNVLRSITFTTNLKAHGPYGQKVGTPFSSANVVGNEIVGFLGRSGYYVDAIGTYNRHK

Entity 2 Entity 2 non-polymer

Description description	1,2-ETHANEDIOL
Molecular weight formula_weight	62.1 kDa
Source method src_method	syn
Copy count entity_count	9

Entity 3 Entity 3 non-polymer

Description description	IMIDAZOLE
Molecular weight formula_weight	69.1 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 4 Entity 4 non-polymer

Description description	D-MALATE
Molecular weight formula_weight	134.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	589

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6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1ouwa_
Class class	b — All beta proteins
Fold Fold fold	b.77 — beta-Prism I
Superfamily Superfamily superfamily	b.77.3 — Mannose-binding lectins
Family Family family	b.77.3.1 — Mannose-binding lectins

Domain ID domain_id	d1ouwb_
Class class	b — All beta proteins
Fold Fold fold	b.77 — beta-Prism I
Superfamily Superfamily superfamily	b.77.3 — Mannose-binding lectins
Family Family family	b.77.3.1 — Mannose-binding lectins

Domain ID domain_id	d1ouwc_
Class class	b — All beta proteins
Fold Fold fold	b.77 — beta-Prism I
Superfamily Superfamily superfamily	b.77.3 — Mannose-binding lectins
Family Family family	b.77.3.1 — Mannose-binding lectins

Domain ID domain_id	d1ouwd_
Class class	b — All beta proteins
Fold Fold fold	b.77 — beta-Prism I
Superfamily Superfamily superfamily	b.77.3 — Mannose-binding lectins
Family Family family	b.77.3.1 — Mannose-binding lectins

CATH v4.4 (4 domains)

Domain ID domain_id	1ouwA00
Class class	2 — Mainly Beta
Architecture architecture	100 — Aligned Prism
Topology topology	10 — Vitelline Membrane Outer Layer Protein I, subunit A
Homologous superfamily homologous superfamily	30 — Jacalin-like lectin domain

Domain ID domain_id	1ouwB00
Class class	2 — Mainly Beta
Architecture architecture	100 — Aligned Prism
Topology topology	10 — Vitelline Membrane Outer Layer Protein I, subunit A
Homologous superfamily homologous superfamily	30 — Jacalin-like lectin domain

Domain ID domain_id	1ouwC00
Class class	2 — Mainly Beta
Architecture architecture	100 — Aligned Prism
Topology topology	10 — Vitelline Membrane Outer Layer Protein I, subunit A
Homologous superfamily homologous superfamily	30 — Jacalin-like lectin domain

Domain ID domain_id	1ouwD00
Class class	2 — Mainly Beta
Architecture architecture	100 — Aligned Prism
Topology topology	10 — Vitelline Membrane Outer Layer Protein I, subunit A
Homologous superfamily homologous superfamily	30 — Jacalin-like lectin domain

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Unit-cell length a length_a	30.562 Å
Unit-cell length b length_b	51.792 Å
Unit-cell length c length_c	79.780 Å
Unit-cell angle α angle_alpha	104.99 °
Unit-cell angle β angle_beta	94.36 °
Unit-cell angle γ angle_gamma	94.85 °
Molecules per unit cell Z z_pdb	4

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

Resolution resolution	1.370 Å
Low-resolution limit resolution_low	25.000 Å
R factor r_factor	0.1531
R_work r_work	0.1526
R_free r_free	0.1797

Crystal structure of Calystegia sepium agglutinin

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

lectin

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

1ouw__assembly_2__model_1

1ouw__assembly_2__model_1 | I(q)

1ouw__assembly_2__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)

Crystal structure of Calystegia sepium agglutinin

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

lectin

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

1ouw__assembly_2__model_1

1ouw__assembly_2__model_1 | I(q)

1ouw__assembly_2__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)