SAXSdb — 2wra

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

LECTIN

BURKHOLDERIA CENOCEPACIA

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Other combination	Homooligomer	Protein 2 其他Polymer 2	alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose × 2 CALCIUM ION × 4 SULFATE ION × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	B4EH87_BURCJ
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–128； UniProt 2–129

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	2wra
Deposition date deposition_date	2009-09-01
Structure title title	BclA lectin from Burkholderia cenocepacia complexed with aMan1(aMan1- 6)-3Man trisaccharide
Keywords keywords	SUGAR BINDING PROTEIN, BACTERIAL LECTIN, OLIGOSACCHARIDES; 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.

2wra__assembly_1__model_1

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

Download this curve (.dat)

2wra__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2wra__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	19.10 Å
Rg (electron density)	17.59 Å
Total Rg	18.68 Å
Atom count	1946
Residues	244
Excluded volume	34142 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2wra__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 (5)

Entity 1 Entity 1 polymer

Description description	LECTIN
Molecular weight formula_weight	13779.0 kDa
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	1218

ADSQTSSNRAGEFSIPPNTDFRAIFFANAAEQQHIKLFIGDSQEPAAYHKLTTRDGPREATLNSGNGKIRFEVSVNGKPSATDARLAPINGKKSDGSPFTVNFGIVVSEDGHDSDYNDGIVVLQWPIG

Source Source

Source organism organism	BURKHOLDERIA CENOCEPACIA
NCBI taxonomy ID ncbi_taxonomy_id	216591
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 branched

Description description	alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose
Molecular weight formula_weight	504.4 kDa
Source method src_method	man
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 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	178

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d2wraa_
Class class	b — All beta proteins
Fold Fold fold	b.115 — Calcium-mediated lectin
Superfamily Superfamily superfamily	b.115.1 — Calcium-mediated lectin
Family Family family	b.115.1.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id	2wraA00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	400 — Calcium-mediated lectin

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Unit-cell length a length_a	66.296 Å
Unit-cell length b length_b	66.296 Å
Unit-cell length c length_c	46.159 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 31 2 1
Space-group number int_tables_number	152
Crystal system crystal_system	—

Resolution resolution	1.100 Å
Low-resolution limit resolution_low	57.450 Å
R factor r_factor	0.1450
R_work r_work	0.1436
R_free r_free	0.1730

BclA lectin from Burkholderia cenocepacia complexed with aMan1(aMan1- 6)-3Man trisaccharide

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

2wra__assembly_1__model_1

2wra__assembly_1__model_1 | I(q)

2wra__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 branched

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (1)

BclA lectin from Burkholderia cenocepacia complexed with aMan1(aMan1- 6)-3Man trisaccharide

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

2wra__assembly_1__model_1

2wra__assembly_1__model_1 | I(q)

2wra__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 branched

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (1)