SAXSdb — 3zi8

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

PUTATIVE FUCOSE-BINDING LECTIN PROTEIN

RALSTONIA SOLANACEARUM

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 3	beta-L-fucopyranose × 3 MAGNESIUM ION × 3 (4R)-2-METHYLPENTANE-2,4-DIOL × 3 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	D8NA05_RALSL
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–90； UniProt 2–91

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	3zi8
Deposition date deposition_date	2013-01-07
Structure title title	Structure of the R17A mutant of the Ralstonia soleanacerum lectin at 1.5 Angstrom in complex with L-fucose
Keywords keywords	SUGAR BINDING PROTEIN, MULTIVALENCY; 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.

3zi8__assembly_1__model_1

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

Download this curve (.dat)

3zi8__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3zi8__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	18.26 Å
Rg (electron density)	17.10 Å
Total Rg	18.15 Å
Atom count	2103
Residues	270
Excluded volume	36799 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3zi8__assembly_1__model_1`	trimeric （3）	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	PUTATIVE FUCOSE-BINDING LECTIN PROTEIN
Molecular weight formula_weight	9647.4 kDa
Mutation mutation	YES
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	843

SSVQTAATSWGTVPSIAVYTANNGKITERCWDGKGWYTGAFNEPGDNVSVTSWLVGSAIHIRVYASTGTTTTEWCWDGNGWTKGAYTATN

Source Source

Source organism organism	RALSTONIA SOLANACEARUM
NCBI taxonomy ID ncbi_taxonomy_id	305
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 non-polymer

Description description	beta-L-fucopyranose
Molecular weight formula_weight	164.2 kDa
Source method src_method	man
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	(4R)-2-METHYLPENTANE-2,4-DIOL
Molecular weight formula_weight	118.2 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	105

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6. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	3zi8A01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	128 — Lipocalin
Homologous superfamily homologous superfamily	190 —

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Unit-cell length a length_a	72.399 Å
Unit-cell length b length_b	72.399 Å
Unit-cell length c length_c	35.990 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	6

Space group space_group	P 3 2 1
Space-group number int_tables_number	150
Crystal system crystal_system	—

Resolution resolution	1.500 Å
Low-resolution limit resolution_low	36.200 Å
R factor r_factor	0.1351
R_work r_work	0.1336
R_free r_free	0.1656

Structure of the R17A mutant of the Ralstonia soleanacerum lectin at 1.5 Angstrom in complex with L-fucose

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

PUTATIVE FUCOSE-BINDING LECTIN PROTEIN

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

3zi8__assembly_1__model_1

3zi8__assembly_1__model_1 | I(q)

3zi8__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

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) 1 domains

CATH v4.4 (1 domains)

7. Citations (1)

Structure of the R17A mutant of the Ralstonia soleanacerum lectin at 1.5 Angstrom in complex with L-fucose

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

PUTATIVE FUCOSE-BINDING LECTIN PROTEIN

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

3zi8__assembly_1__model_1

3zi8__assembly_1__model_1 | I(q)

3zi8__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

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) 1 domains

CATH v4.4 (1 domains)

7. Citations (1)