SAXSdb — 4akc

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

AGGLUTININ ALPHA CHAIN

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Other combination	Heteromer	Protein 8 其他Polymer 4	AGGLUTININ BETA-4 CHAIN × 4 （Q9S8T0） beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-alpha-D-galactopyranose × 4 water × 6	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	LECA_ARTIN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–133； UniProt 1–133 Author chain C； PDBConstruct 1–133； UniProt 1–133 Author chain E； PDBConstruct 1–133； UniProt 1–133 Author chain G； PDBConstruct 1–133； UniProt 1–133

AGGLUTININ BETA-4 CHAIN

OrganismNot specified

UniProt Q9S8T0

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Other combination	Heteromer	Protein 8 其他Polymer 4	AGGLUTININ ALPHA CHAIN × 4 （P18670） beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-alpha-D-galactopyranose × 4 water × 6	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	LECB4_ARTIN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–19； UniProt 1–19 Author chain D； PDBConstruct 1–19； UniProt 1–19 Author chain F； PDBConstruct 1–19； UniProt 1–19 Author chain H； PDBConstruct 1–19； UniProt 1–19

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	4akc
Deposition date deposition_date	2012-02-22
Structure title title	Structure of Galactose Binding lectin from Champedak (CGB) with Gal(beta)1,3-GalNac
Keywords keywords	SUGAR BINDING PROTEIN, MANNOSE; 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.

4akc__assembly_1__model_1

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

Download this curve (.dat)

4akc__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4akc__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	27.53 Å
Rg (electron density)	26.67 Å
Total Rg	27.46 Å
Atom count	4689
Residues	593
Excluded volume	84152 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4akc__assembly_1__model_1`	octameric （8）	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 (4)

Entity 1 Entity 1 polymer

Description description	AGGLUTININ ALPHA CHAIN
Molecular weight formula_weight	14662.5 kDa
Source method src_method	nat
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C,E,G
Atom count atom_count	4740

GKAFDDGAFTGIREINLSYNKETAIGDFQVVYDLNGSPYVGENHKSFITGFTPVKISLDFPSEYIMEVSGYTGKVSGYVVVRSLTFKTNKKTYGPYGVTSGTPFSLPIENGLIVGFKGSIGYWLDYFSMYLSL

Entity 2 Entity 2 polymer

Description description	AGGLUTININ BETA-4 CHAIN
Molecular weight formula_weight	2158.3 kDa
Source method src_method	nat
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D,F,H

NEQSGISQTVIVGPWGAQVST

Entity 3 Entity 3 branched

Description description	beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-alpha-D-galactopyranose
Molecular weight formula_weight	383.3 kDa
Source method src_method	man
Copy count entity_count	4

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	51

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6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id	4akcA00
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	4akcC00
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	4akcE00
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	4akcG00
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	76.287 Å
Unit-cell length b length_b	121.673 Å
Unit-cell length c length_c	77.563 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	16

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	30.490 Å
R factor r_factor	0.2005
R_work r_work	0.1982
R_free r_free	0.2459

Structure of Galactose Binding lectin from Champedak (CGB) with Gal(beta)1,3-GalNac

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

AGGLUTININ ALPHA CHAIN

State in the Current Structure

Other States of the Same Protein in the Database

AGGLUTININ BETA-4 CHAIN

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

4akc__assembly_1__model_1

4akc__assembly_1__model_1 | I(q)

4akc__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 polymer

Polymer Polymer

Entity 3 Entity 3 branched

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

7. Citations (1)

Structure of Galactose Binding lectin from Champedak (CGB) with Gal(beta)1,3-GalNac

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

AGGLUTININ ALPHA CHAIN

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

AGGLUTININ BETA-4 CHAIN

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

4akc__assembly_1__model_1

4akc__assembly_1__model_1 | I(q)

4akc__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 polymer

Polymer Polymer

Entity 3 Entity 3 branched

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

7. Citations (1)