1slq

Crystal structure of the trimeric state of the rhesus rotavirus VP4 membrane interaction domain, VP5CT

Method: X-RAY DIFFRACTION

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

VP4

Rhesus rotavirus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 3	No other associated polymer	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 3	No other associated polymer	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 6	No other associated polymer	Consistent with protein count
4	Protein homooligomer	Homooligomer	Protein 6	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q91HI9_ROTRH
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–278； UniProt 248–525 Author chain B； PDBConstruct 1–278； UniProt 248–525 Author chain C； PDBConstruct 1–278； UniProt 248–525 Author chain D； PDBConstruct 1–278； UniProt 248–525 Author chain E； PDBConstruct 1–278； UniProt 248–525 Author chain F； PDBConstruct 1–278； UniProt 248–525

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	1slq
Deposition date deposition_date	2004-03-06
Structure title title	Crystal structure of the trimeric state of the rhesus rotavirus VP4 membrane interaction domain, VP5CT
Keywords keywords	;beta sandwich, greek key, alpha helical triple coiled-coil, membrane penetration protein, non-enveloped virus, spike protein, 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.

1slq__assembly_1__model_1

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

Download this curve (.dat)

1slq__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1slq__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	29.60 Å
Rg (electron density)	28.72 Å
Total Rg	29.62 Å
Atom count	6408
Residues	805
Excluded volume	113290 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1slq__assembly_1__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1slq__assembly_2__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`1slq__assembly_3__model_1`	hexameric （6）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`1slq__assembly_4__model_1`	hexameric （6）	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 (1)

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6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d1slqa_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.47 — VP4 membrane interaction domain
Superfamily Superfamily superfamily	f.47.1 — VP4 membrane interaction domain
Family Family family	f.47.1.1 — VP4 membrane interaction domain

Domain ID domain_id	d1slqb_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.47 — VP4 membrane interaction domain
Superfamily Superfamily superfamily	f.47.1 — VP4 membrane interaction domain
Family Family family	f.47.1.1 — VP4 membrane interaction domain

Domain ID domain_id	d1slqc_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.47 — VP4 membrane interaction domain
Superfamily Superfamily superfamily	f.47.1 — VP4 membrane interaction domain
Family Family family	f.47.1.1 — VP4 membrane interaction domain

Domain ID domain_id	d1slqd_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.47 — VP4 membrane interaction domain
Superfamily Superfamily superfamily	f.47.1 — VP4 membrane interaction domain
Family Family family	f.47.1.1 — VP4 membrane interaction domain

Domain ID domain_id	d1slqe_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.47 — VP4 membrane interaction domain
Superfamily Superfamily superfamily	f.47.1 — VP4 membrane interaction domain
Family Family family	f.47.1.1 — VP4 membrane interaction domain

Domain ID domain_id	d1slqf_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.47 — VP4 membrane interaction domain
Superfamily Superfamily superfamily	f.47.1 — VP4 membrane interaction domain
Family Family family	f.47.1.1 — VP4 membrane interaction domain

CATH v4.4 (6 domains)

Domain ID domain_id	1slqA02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	170 —

Domain ID domain_id	1slqB02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	170 —

Domain ID domain_id	1slqC02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	170 —

Domain ID domain_id	1slqD02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	170 —

Domain ID domain_id	1slqE02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	170 —

Domain ID domain_id	1slqF02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	170 —

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Unit-cell length a length_a	244.843 Å
Unit-cell length b length_b	244.843 Å
Unit-cell length c length_c	104.778 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	48

Space group space_group	P 42 2 2
Space-group number int_tables_number	93
Crystal system crystal_system	—

Resolution resolution	3.200 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.3100
R_work r_work	0.3080
R_free r_free	0.3380

Description description	VP4
Molecular weight formula_weight	31307.9 kDa
Source method src_method	man
Copy count entity_count	6

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F
Atom count atom_count	12772

Crystal structure of the trimeric state of the rhesus rotavirus VP4 membrane interaction domain, VP5CT

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

VP4

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

1slq__assembly_1__model_1

1slq__assembly_1__model_1 | I(q)

1slq__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

CATH v4.4 (6 domains)

7. Citations (4)

Source organism organism	Rhesus rotavirus
NCBI taxonomy ID ncbi_taxonomy_id	10969
Host organism host_organism	Spodoptera frugiperda

Crystal structure of the trimeric state of the rhesus rotavirus VP4 membrane interaction domain, VP5CT

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

VP4

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

1slq__assembly_1__model_1

1slq__assembly_1__model_1 | I(q)

1slq__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

CATH v4.4 (6 domains)

7. Citations (4)