SAXSdb — 1lj2

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

NONSTRUCTURAL RNA-BINDING PROTEIN 34

Simian rotavirus A/SA11

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	eukaryotic protein synthesis initiation factor × 2 （Q04637） GOLD ION × 3 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	VN34_ROTS1
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–110； UniProt 206–315 Author chain B； PDBConstruct 1–110； UniProt 206–315

eukaryotic protein synthesis initiation factor

OrganismNot specified

UniProt Q04637

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	NONSTRUCTURAL RNA-BINDING PROTEIN 34 × 2 （P03536） GOLD ION × 3 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	IF4G1_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–28； UniProt 172–199 Author chain D； PDBConstruct 1–28； UniProt 172–199

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	1lj2
Deposition date deposition_date	2002-04-18
Structure title title	Recognition of eIF4G by Rotavirus NSP3 reveals a basis for mRNA circularization
Keywords keywords	NSP3; homodimer; eIF4G; Rotavirus; translation; mRNA; closed loop; coiled coil, Viral protein- translation COMPLEX; Viral protein/ translation
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.

1lj2__assembly_1__model_1

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

Download this curve (.dat)

1lj2__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1lj2__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	26.38 Å
Rg (electron density)	26.01 Å
Total Rg	26.85 Å
Atom count	2131
Residues	265
Excluded volume	37733 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1lj2__assembly_1__model_1`	tetrameric （4）	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	NONSTRUCTURAL RNA-BINDING PROTEIN 34
Molecular weight formula_weight	12842.4 kDa
Mutation mutation	C306S C314S
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	2327

MHSLQNVIPQQQAHIAELQVYNNKLERDLQNKIGSLTSSIEWYLRSMELDPEIKADIEQQINSIDAINPLHAFDDLESVIRNLISDYDKLFLMFKGLIQRSNYQYSFGSE

Source Source

Source organism organism	Simian rotavirus A/SA11
NCBI taxonomy ID ncbi_taxonomy_id	10923
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	eukaryotic protein synthesis initiation factor
Molecular weight formula_weight	3203.7 kDa
Source method src_method	syn
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,D

APKRERKTIRIRDPNQGGKDITEEIMSG

Entity 3 Entity 3 non-polymer

Description description	GOLD ION
Molecular weight formula_weight	197.0 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	196

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1lj2a_
Class class	h — Coiled coil proteins
Fold Fold fold	h.1 — Parallel coiled-coil
Superfamily Superfamily superfamily	h.1.13 — Rotavirus nonstructural proteins
Family Family family	h.1.13.2 — NSP3 C-terminal domain, NS34

Domain ID domain_id	d1lj2b_
Class class	h — Coiled coil proteins
Fold Fold fold	h.1 — Parallel coiled-coil
Superfamily Superfamily superfamily	h.1.13 — Rotavirus nonstructural proteins
Family Family family	h.1.13.2 — NSP3 C-terminal domain, NS34

CATH v4.4 (2 domains)

Domain ID domain_id	1lj2A00
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	970 — Nonstructural RNA-binding protein

Domain ID domain_id	1lj2B00
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	970 — Nonstructural RNA-binding protein

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Unit-cell length a length_a	59.690 Å
Unit-cell length b length_b	74.040 Å
Unit-cell length c length_c	77.460 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	8

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.380 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	—
R_work r_work	0.2210
R_free r_free	0.2720

Recognition of eIF4G by Rotavirus NSP3 reveals a basis for mRNA circularization

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

NONSTRUCTURAL RNA-BINDING PROTEIN 34

State in the Current Structure

Other States of the Same Protein in the Database

eukaryotic protein synthesis initiation factor

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

1lj2__assembly_1__model_1

1lj2__assembly_1__model_1 | I(q)

1lj2__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

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)

Recognition of eIF4G by Rotavirus NSP3 reveals a basis for mRNA circularization

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

NONSTRUCTURAL RNA-BINDING PROTEIN 34

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

eukaryotic protein synthesis initiation factor

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

1lj2__assembly_1__model_1

1lj2__assembly_1__model_1 | I(q)

1lj2__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

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)