SAXSdb — 5a49

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

MATERNAL EFFECT PROTEIN OSKAR

DROSOPHILA MELANOGASTER

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count
4	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count
5	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count
6	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	OSKA_DROME
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 6–89； UniProt 139–222 Author chain B； PDBConstruct 6–89； UniProt 139–222 Author chain C； PDBConstruct 6–89； UniProt 139–222 Author chain D； PDBConstruct 6–89； UniProt 139–222 Author chain E； PDBConstruct 6–89； UniProt 139–222 Author chain F； PDBConstruct 6–89； UniProt 139–222 Author chain G； PDBConstruct 6–89； UniProt 139–222 Author chain H； PDBConstruct 6–89； UniProt 139–222 Author chain I； PDBConstruct 6–89； UniProt 139–222 Author chain J； PDBConstruct 6–89； UniProt 139–222

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	5a49
Deposition date deposition_date	2015-06-05
Structure title title	Crystal structure of the LOTUS domain (aa 139-222) of Drosophila Oskar in C222
Keywords keywords	PROTEIN BINDING, OST-HTH DOMAIN, DIMER, WINGED HELIX-TURN-HELIX, VASA, PROTEIN BINDING INTERACTION, GERM PLASM; PROTEIN BINDING
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.

5a49__assembly_4__model_1

Assembly 4 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

5a49__assembly_4__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

5a49__assembly_4__model_1 | P(r) · Pending

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

Rg（Guinier）	17.03 Å
Rg (electron density)	16.03 Å
Total Rg	16.96 Å
Atom count	1053
Residues	134
Excluded volume	18796 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`5a49__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`5a49__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`5a49__assembly_3__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`5a49__assembly_4__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
5	1	`5a49__assembly_5__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
6	1	`5a49__assembly_6__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 (2)

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6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id	5a49E00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily	610 — LOTUS domain-like

Domain ID domain_id	5a49F00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily	610 — LOTUS domain-like

Domain ID domain_id	5a49G00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily	610 — LOTUS domain-like

Domain ID domain_id	5a49J00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily	610 — LOTUS domain-like

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Unit-cell length a length_a	134.060 Å
Unit-cell length b length_b	198.630 Å
Unit-cell length c length_c	89.120 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	80

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

Resolution resolution	2.098 Å
Low-resolution limit resolution_low	41.359 Å
R factor r_factor	0.1945
R_work r_work	0.1938
R_free r_free	0.2148

Description description	MATERNAL EFFECT PROTEIN OSKAR
Molecular weight formula_weight	9835.1 kDa
Source method src_method	man
Copy count entity_count	10

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J
Atom count atom_count	5973

Crystal structure of the LOTUS domain (aa 139-222) of Drosophila Oskar in C222

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

MATERNAL EFFECT PROTEIN OSKAR

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

5a49__assembly_4__model_1

5a49__assembly_4__model_1 | I(q)

5a49__assembly_4__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

7. Citations (1)

Source organism organism	DROSOPHILA MELANOGASTER
Common name common_name	FRUIT FLY
NCBI taxonomy ID ncbi_taxonomy_id	7227
Host organism host_organism	ESCHERICHIA COLI

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	193

Crystal structure of the LOTUS domain (aa 139-222) of Drosophila Oskar in C222

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

MATERNAL EFFECT PROTEIN OSKAR

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

5a49__assembly_4__model_1

5a49__assembly_4__model_1 | I(q)

5a49__assembly_4__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

7. Citations (1)