2v1c

Crystal structure and mutational study of RecOR provide insight into its role in DNA repair

Method: X-RAY DIFFRACTION

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

RECOMBINATION PROTEIN RECR

DEINOCOCCUS RADIODURANS

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 6	HYPOTHETICAL PROTEIN × 2 （Q9RW50） ZINC ION × 6	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	RECR_DEIRA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–220； UniProt 1–220 Author chain B； PDBConstruct 1–220； UniProt 1–220

HYPOTHETICAL PROTEIN

DEINOCOCCUS RADIODURANS

UniProt Q9RW50

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 6	RECOMBINATION PROTEIN RECR × 4 （Q9ZNA2） ZINC ION × 6	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9RW50_DEIRA
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； 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	2v1c
Deposition date deposition_date	2007-05-23
Structure title title	Crystal structure and mutational study of RecOR provide insight into its role in DNA repair
Keywords keywords	;RECOMBINATION, HOMOLOGOUS RECOMBINATION, RECFOR PATHWAY, DNA RECOMBINATION, DNA BINDING, ZINC-FINGER, METAL-BINDING, RECOR COMPLEX, HYPOTHETICAL PROTEIN, DEINOCOCCUS RADIODURANS, RECR, ZINC, RECO, DNA DAMAGE, DNA REPAIR ;; RECOMBINATION
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.

2v1c__assembly_1__model_1

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

Download this curve (.dat)

2v1c__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2v1c__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	35.91 Å
Rg (electron density)	35.09 Å
Total Rg	35.76 Å
Atom count	9562
Residues	1254
Excluded volume	170930 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2v1c__assembly_1__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 (3)

Entity 1 Entity 1 polymer

Description description	RECOMBINATION PROTEIN RECR
Molecular weight formula_weight	23752.2 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	4781

MKYPPSLVSLIRELSRLPGIGPKSAQRLAFHLFEQPREDIERLASALLEAKRDLHVCPICFNITDAEKCDVCADPSRDQRTICVVEEPGDVIALERSGEYRGLYHVLHGVLSPMNGVGPDKLHIKPLLPRVGQGMEVILATGTTVEGDATALYLQRLLEPLGAAISRIAYGVPVGGSLEYTDEVTLGRALTGRQTVSKPQPPQRPGDEDGADGAAVPASR

Source Source

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

Entity 2 Entity 2 polymer

Description description	HYPOTHETICAL PROTEIN
Molecular weight formula_weight	26376.4 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

MRSRTANRSGIVIRRRVTPAGDIIVTLLTPQGKLKAIARGGVKGPLSSSLNLFHHVGVQVYQGPHNDLASVKQAVLEGALPTLAEPERYAFAHLMAEFADALFQEGEFSEQAFDLFAASLRGVAHQPDPEWVALVMSYKLLGLAGVIPQTARCARCGAPDPEHPDPLGGQLLCSKCAALPPYPPAVLDFLRHAVRRTVRASFEQPVPSADRPALWRALEKFVTVQVGGVHSWRQLVPSGVPVLS

Source Source

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

Entity 3 Entity 3 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	3

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6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d2v1ca1
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.49 — Recombination protein RecR
Superfamily Superfamily superfamily	e.49.1 — Recombination protein RecR
Family Family family	e.49.1.1 — Recombination protein RecR

Domain ID domain_id	d2v1cb1
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.49 — Recombination protein RecR
Superfamily Superfamily superfamily	e.49.1 — Recombination protein RecR
Family Family family	e.49.1.1 — Recombination protein RecR

CATH v4.4 (10 domains)

Domain ID domain_id	2v1cA01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily	420 — RecR Domain 1

Domain ID domain_id	2v1cA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	60 — Wheat Germ Agglutinin (Isolectin 2); domain 1
Homologous superfamily homologous superfamily	80 —

Domain ID domain_id	2v1cA03
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1360 — Dna Topoisomerase Vi A Subunit; Chain: A, domain 2
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	2v1cB01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily	420 — RecR Domain 1

Domain ID domain_id	2v1cB02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	60 — Wheat Germ Agglutinin (Isolectin 2); domain 1
Homologous superfamily homologous superfamily	80 —

Domain ID domain_id	2v1cB03
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1360 — Dna Topoisomerase Vi A Subunit; Chain: A, domain 2
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	2v1cB04
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	240 —

Domain ID domain_id	2v1cC01
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	2v1cC02
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	2v1cC03
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	144.000 Å
Unit-cell length b length_b	83.200 Å
Unit-cell length c length_c	66.600 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	106.90 °
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	3.800 Å
Low-resolution limit resolution_low	71.250 Å
R factor r_factor	0.4580
R_work r_work	0.4590
R_free r_free	0.4430

Crystal structure and mutational study of RecOR provide insight into its role in DNA repair

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

RECOMBINATION PROTEIN RECR

State in the Current Structure

Other States of the Same Protein in the Database

HYPOTHETICAL PROTEIN

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

2v1c__assembly_1__model_1

2v1c__assembly_1__model_1 | I(q)

2v1c__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 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (2 domains)

CATH v4.4 (10 domains)

7. Citations (1)

Crystal structure and mutational study of RecOR provide insight into its role in DNA repair

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

RECOMBINATION PROTEIN RECR

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

HYPOTHETICAL PROTEIN

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

2v1c__assembly_1__model_1

2v1c__assembly_1__model_1 | I(q)

2v1c__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 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (2 domains)

CATH v4.4 (10 domains)

7. Citations (1)