SAXSdb — 3s6z

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

Outer capsid protein sigma-1

Reovirus type 3

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Other combination	Homooligomer	Protein 3 其他Polymer 2	N-acetyl-alpha-neuraminic acid-(2-8)-N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose × 2 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	SIGM1_REOVD
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 40–325； UniProt 170–455 Author chain B； PDBConstruct 40–325； UniProt 170–455 Author chain C； PDBConstruct 40–325； UniProt 170–455

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	3s6z
Deposition date deposition_date	2011-05-26
Structure title title	Structure of reovirus attachment protein sigma1 in complex with alpha-2,8-disialyllactose
Keywords keywords	;triple beta-spiral, beta-barrel, beta-spiral repeat, greek key motif, trimer, Viral attachment protein, sialic acid receptor Junctional adhesion molecule A, Viral capsid, VIRAL PROTEIN ;; VIRAL 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.

3s6z__assembly_1__model_1

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

Download this curve (.dat)

3s6z__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3s6z__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	60.34 Å
Rg (electron density)	62.02 Å
Total Rg	61.77 Å
Atom count	6767
Residues	877
Excluded volume	119690 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3s6z__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 (3)

Entity 1 Entity 1 polymer

Description description	Outer capsid protein sigma-1
Molecular weight formula_weight	35360.8 kDa
Mutation mutation	T249I
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	7499

QIEDKIEEILSKIYHIENEIARIKKLIGEGSGRPVLNQGVTSAGAPLSIRNNRMTMGLNDGLTLSGNNLAIRLPGNTGLNIQNGGLQFRFNTDQFQIVNNNLTLKTTVFDSINSRIGAIEQSYVASAVTPLRLNSSTKVLDMLIDSSTLEINSSGQLTVRSTSPNLRYPIADVSGGIGMSPNYRFRQSMWIGIVSYSGSGLNWRVQVNSDIFIVDDYIHICLPAFDGFSIADGGDLSLNFVTGLLPPLLTGDTEPAFHNDVVTYGAQTVAIGLSSGGTPQYMSKNLWVEQWQDGVLRLRVEGGGSITHSNSKWPAMTVSYPRSFT

Source Source

Source organism organism	Reovirus type 3
Common name common_name	Mammalian orthoreovirus 3
NCBI taxonomy ID ncbi_taxonomy_id	10886
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 branched

Description description	N-acetyl-alpha-neuraminic acid-(2-8)-N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose
Molecular weight formula_weight	762.7 kDa
Source method src_method	man
Copy count entity_count	2

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	715

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6. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	3s6zC01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	90 — Adenovirus Type 5 Fiber Protein (Receptor Binding Domain)
Homologous superfamily homologous superfamily	20 — Virus attachment protein , globular domain

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Unit-cell length a length_a	87.150 Å
Unit-cell length b length_b	333.180 Å
Unit-cell length c length_c	58.490 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	12

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

Resolution resolution	2.280 Å
Low-resolution limit resolution_low	48.058 Å
R factor r_factor	0.1753
R_work r_work	0.1730
R_free r_free	0.2194

Structure of reovirus attachment protein sigma1 in complex with alpha-2,8-disialyllactose

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

Outer capsid protein sigma-1

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

3s6z__assembly_1__model_1

3s6z__assembly_1__model_1 | I(q)

3s6z__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

Source Source

Entity 2 Entity 2 branched

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

7. Citations (1)

Structure of reovirus attachment protein sigma1 in complex with alpha-2,8-disialyllactose

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

Outer capsid protein sigma-1

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

3s6z__assembly_1__model_1

3s6z__assembly_1__model_1 | I(q)

3s6z__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

Source Source

Entity 2 Entity 2 branched

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

7. Citations (1)