5jrb

Rad52(1-212) K102A/K133A/E202A mutant

Method: X-RAY DIFFRACTION

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

DNA repair protein RAD52 homolog

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 11	water × 11	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	RAD52_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–215； UniProt 1–212 Author chain B； PDBConstruct 4–215； UniProt 1–212 Author chain C； PDBConstruct 4–215； UniProt 1–212 Author chain D； PDBConstruct 4–215； UniProt 1–212 Author chain E； PDBConstruct 4–215； UniProt 1–212 Author chain F； PDBConstruct 4–215； UniProt 1–212 Author chain G； PDBConstruct 4–215； UniProt 1–212 Author chain H； PDBConstruct 4–215； UniProt 1–212 Author chain I； PDBConstruct 4–215； UniProt 1–212 Author chain J； PDBConstruct 4–215； UniProt 1–212 Author chain K； PDBConstruct 4–215； UniProt 1–212

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	5jrb
Deposition date deposition_date	2016-05-06
Structure title title	Rad52(1-212) K102A/K133A/E202A mutant
Keywords keywords	DNA annealing protein, ssDNA binding, multimeric ring formation, DNA BINDING PROTEIN; DNA BINDING 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.

5jrb__assembly_1__model_1

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

Download this curve (.dat)

5jrb__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

5jrb__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	40.68 Å
Rg (electron density)	40.13 Å
Total Rg	40.79 Å
Atom count	15852
Residues	2028
Excluded volume	279830 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`5jrb__assembly_1__model_1`	undecameric （11）	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) 22 domains

SCOP 2.08 (11 domains)

Domain ID domain_id	d5jrba_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.50 — dsRBD-like
Superfamily Superfamily superfamily	d.50.1 — dsRNA-binding domain-like
Family Family family	d.50.1.3 — The homologous-pairing domain of Rad52 recombinase

Domain ID domain_id	d5jrbb_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.50 — dsRBD-like
Superfamily Superfamily superfamily	d.50.1 — dsRNA-binding domain-like
Family Family family	d.50.1.3 — The homologous-pairing domain of Rad52 recombinase

Domain ID domain_id	d5jrbc_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.50 — dsRBD-like
Superfamily Superfamily superfamily	d.50.1 — dsRNA-binding domain-like
Family Family family	d.50.1.3 — The homologous-pairing domain of Rad52 recombinase

Domain ID domain_id	d5jrbd_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.50 — dsRBD-like
Superfamily Superfamily superfamily	d.50.1 — dsRNA-binding domain-like
Family Family family	d.50.1.3 — The homologous-pairing domain of Rad52 recombinase

Domain ID domain_id	d5jrbe_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.50 — dsRBD-like
Superfamily Superfamily superfamily	d.50.1 — dsRNA-binding domain-like
Family Family family	d.50.1.3 — The homologous-pairing domain of Rad52 recombinase

Domain ID domain_id	d5jrbf_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.50 — dsRBD-like
Superfamily Superfamily superfamily	d.50.1 — dsRNA-binding domain-like
Family Family family	d.50.1.3 — The homologous-pairing domain of Rad52 recombinase

Domain ID domain_id	d5jrbg_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.50 — dsRBD-like
Superfamily Superfamily superfamily	d.50.1 — dsRNA-binding domain-like
Family Family family	d.50.1.3 — The homologous-pairing domain of Rad52 recombinase

Domain ID domain_id	d5jrbh_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.50 — dsRBD-like
Superfamily Superfamily superfamily	d.50.1 — dsRNA-binding domain-like
Family Family family	d.50.1.3 — The homologous-pairing domain of Rad52 recombinase

Domain ID domain_id	d5jrbi_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.50 — dsRBD-like
Superfamily Superfamily superfamily	d.50.1 — dsRNA-binding domain-like
Family Family family	d.50.1.3 — The homologous-pairing domain of Rad52 recombinase

Domain ID domain_id	d5jrbj_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.50 — dsRBD-like
Superfamily Superfamily superfamily	d.50.1 — dsRNA-binding domain-like
Family Family family	d.50.1.3 — The homologous-pairing domain of Rad52 recombinase

Domain ID domain_id	d5jrbk_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.50 — dsRBD-like
Superfamily Superfamily superfamily	d.50.1 — dsRNA-binding domain-like
Family Family family	d.50.1.3 — The homologous-pairing domain of Rad52 recombinase

CATH v4.4 (11 domains)

Domain ID domain_id	5jrbA01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	390 — Enolase-like; domain 1
Homologous superfamily homologous superfamily	80 — DNA repair protein Rad52/59/22

Domain ID domain_id	5jrbB01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	390 — Enolase-like; domain 1
Homologous superfamily homologous superfamily	80 — DNA repair protein Rad52/59/22

Domain ID domain_id	5jrbC01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	390 — Enolase-like; domain 1
Homologous superfamily homologous superfamily	80 — DNA repair protein Rad52/59/22

Domain ID domain_id	5jrbD01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	390 — Enolase-like; domain 1
Homologous superfamily homologous superfamily	80 — DNA repair protein Rad52/59/22

Domain ID domain_id	5jrbE01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	390 — Enolase-like; domain 1
Homologous superfamily homologous superfamily	80 — DNA repair protein Rad52/59/22

Domain ID domain_id	5jrbF01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	390 — Enolase-like; domain 1
Homologous superfamily homologous superfamily	80 — DNA repair protein Rad52/59/22

Domain ID domain_id	5jrbG01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	390 — Enolase-like; domain 1
Homologous superfamily homologous superfamily	80 — DNA repair protein Rad52/59/22

Domain ID domain_id	5jrbH01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	390 — Enolase-like; domain 1
Homologous superfamily homologous superfamily	80 — DNA repair protein Rad52/59/22

Domain ID domain_id	5jrbI01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	390 — Enolase-like; domain 1
Homologous superfamily homologous superfamily	80 — DNA repair protein Rad52/59/22

Domain ID domain_id	5jrbJ01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	390 — Enolase-like; domain 1
Homologous superfamily homologous superfamily	80 — DNA repair protein Rad52/59/22

Domain ID domain_id	5jrbK01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	390 — Enolase-like; domain 1
Homologous superfamily homologous superfamily	80 — DNA repair protein Rad52/59/22

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Unit-cell length a length_a	110.955 Å
Unit-cell length b length_b	98.516 Å
Unit-cell length c length_c	116.367 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	91.99 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	22

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.405 Å
Low-resolution limit resolution_low	49.258 Å
R factor r_factor	0.2261
R_work r_work	0.2237
R_free r_free	0.2731

Description description	DNA repair protein RAD52 homolog
Molecular weight formula_weight	23539.5 kDa
Mutation mutation	K102A, K133A, E202A
Source method src_method	man
Copy count entity_count	11

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J,K
Atom count atom_count	16252

Rad52(1-212) K102A/K133A/E202A mutant

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

DNA repair protein RAD52 homolog

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

5jrb__assembly_1__model_1

5jrb__assembly_1__model_1 | I(q)

5jrb__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 22 domains

SCOP 2.08 (11 domains)

CATH v4.4 (11 domains)

7. Citations (1)

Source organism organism	Homo sapiens
Common name common_name	Human
NCBI taxonomy ID ncbi_taxonomy_id	9606
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	400

Rad52(1-212) K102A/K133A/E202A mutant

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

DNA repair protein RAD52 homolog

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

5jrb__assembly_1__model_1

5jrb__assembly_1__model_1 | I(q)

5jrb__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 22 domains

SCOP 2.08 (11 domains)

CATH v4.4 (11 domains)

7. Citations (1)