SAXSdb — 1w3s

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

HYPOTHETICAL PROTEIN DR0819

DEINOCOCCUS RADIODURANS

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	ZINC ION × 1 water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	ZINC ION × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9RW50
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–244； UniProt 1–244 Author chain B； PDBConstruct 1–244； UniProt 1–244

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	1w3s
Deposition date deposition_date	2004-07-18
Structure title title	The crystal structure of RecO from Deinococcus radiodurans.
Keywords keywords	DNA REPAIR, SAD, CYS4 ZINC FINGER, OB-FOLD, RECO; DNA REPAIR
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.

1w3s__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1w3s__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1w3s__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	20.64 Å
Rg (electron density)	19.54 Å
Total Rg	20.63 Å
Atom count	1767
Residues	231
Excluded volume	31533 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1w3s__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1w3s__assembly_2__model_1`	monomeric （1）	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	HYPOTHETICAL PROTEIN DR0819
Molecular weight formula_weight	26376.4 kDa
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	3557

MRSRTANRSGIVIRRRVTPAGDIIVTLLTPQGKLKAIARGGVKGPLSSSLNLFHHVGVQVYQGPHNDLASVKQAVLEGALPTLAEPERYAFAHLMAEFADALFQEGEFSEQAFDLFAASLRGVAHQPDPEWVALVMSYKLLGLAGVIPQTARCARCGAPDPEHPDPLGGQLLCSKCAALPPYPPAVLDFLRHAVRRTVRASFEQPVPSADRPALWRALEKFVTVQVGGVHSWRQLVPSGVPVLS

Source Source

Source organism organism	DEINOCOCCUS RADIODURANS
NCBI taxonomy ID ncbi_taxonomy_id	243230
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
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	23

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6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1w3sa1
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.4 — Nucleic acid-binding proteins
Family Family family	b.40.4.13 — RecO N-terminal domain-like

Domain ID domain_id	d1w3sa2
Class class	g — Small proteins
Fold Fold fold	g.45 — ArfGap/RecO-like zinc finger
Superfamily Superfamily superfamily	g.45.1 — ArfGap/RecO-like zinc finger
Family Family family	g.45.1.2 — RecO C-terminal domain-like

Domain ID domain_id	d1w3sb1
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.4 — Nucleic acid-binding proteins
Family Family family	b.40.4.13 — RecO N-terminal domain-like

Domain ID domain_id	d1w3sb2
Class class	g — Small proteins
Fold Fold fold	g.45 — ArfGap/RecO-like zinc finger
Superfamily Superfamily superfamily	g.45.1 — ArfGap/RecO-like zinc finger
Family Family family	g.45.1.2 — RecO C-terminal domain-like

CATH v4.4 (6 domains)

Domain ID domain_id	1w3sA01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	140 — Nucleic acid-binding proteins

Domain ID domain_id	1w3sA02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1440 — de novo design (two linked rop proteins)
Homologous superfamily homologous superfamily	120 — Recombination protein O, C-terminal domain

Domain ID domain_id	1w3sA03
Class class	6 — Special
Architecture architecture	20 — Other non-globular
Topology topology	220 — Erythroid Transcription Factor GATA-1; Chain A
Homologous superfamily homologous superfamily	20 — Recombination protein O, zinc-binding domain

Domain ID domain_id	1w3sB01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	140 — Nucleic acid-binding proteins

Domain ID domain_id	1w3sB02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1440 — de novo design (two linked rop proteins)
Homologous superfamily homologous superfamily	120 — Recombination protein O, C-terminal domain

Domain ID domain_id	1w3sB03
Class class	6 — Special
Architecture architecture	20 — Other non-globular
Topology topology	220 — Erythroid Transcription Factor GATA-1; Chain A
Homologous superfamily homologous superfamily	20 — Recombination protein O, zinc-binding domain

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Unit-cell length a length_a	134.429 Å
Unit-cell length b length_b	52.351 Å
Unit-cell length c length_c	101.085 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	106.32 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.400 Å
Low-resolution limit resolution_low	95.350 Å
R factor r_factor	0.2270
R_work r_work	0.2250
R_free r_free	0.2670

The crystal structure of RecO from Deinococcus radiodurans.

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

HYPOTHETICAL PROTEIN DR0819

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

1w3s__assembly_2__model_1

1w3s__assembly_2__model_1 | I(q)

1w3s__assembly_2__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 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

CATH v4.4 (6 domains)

7. Citations (1)

The crystal structure of RecO from Deinococcus radiodurans.

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

HYPOTHETICAL PROTEIN DR0819

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

1w3s__assembly_2__model_1

1w3s__assembly_2__model_1 | I(q)

1w3s__assembly_2__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 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

CATH v4.4 (6 domains)

7. Citations (1)