1n0w

Crystal structure of a RAD51-BRCA2 BRC repeat complex

Method: X-RAY DIFFRACTION D_max: 70.0 Å Quality: GOOD

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

DNA repair protein RAD51 homolog 1

Homo sapiens

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 97–339	Fragment：ATPase domain Non-standard monomer：Yes (specific site not provided by mmCIF)	Breast cancer type 2 susceptibility protein × 1 （P51587） peptide linker × 1 ARTIFICIAL GLY-SER-MSE-GLY PEPTIDE × 1 MG MAGNESIUM ION × 1 CL CHLORIDE ION × 1 EDO 1,2-ETHANEDIOL × 5	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.2；291 K；ETHYLENE GLYCOL, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 1.70 Å R-free 0.206

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 1N0W	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1B22 RAD51 (N-TERMINAL DOMAIN) Deposited 1998-12-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–114（114 aa） Fragment：N-TERMINAL DOMAIN	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；303 K；Ionic strength (raw mmCIF value) 100mM NACL；Pressure 1	Resolution not provided
5H1B Human RAD51 presynaptic complex Deposited 2016-10-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 3 PDB declaration: tetrameric	Chain A 1–339（339 aa） Chain B 1–339（339 aa） Chain C 1–339（339 aa）	Mutation：K313Q Mutation：K313Q Mutation：K313Q	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；25mM Tris-HCl, pH 7.5, 50mM KCl, 1mM dithiothreitol, 1mM AMP-PNP and 2mM MgCl2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.40 Å
5H1C Human RAD51 post-synaptic complexes Deposited 2016-10-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 3 PDB declaration: pentameric	Chain A 1–339（339 aa） Chain B 1–339（339 aa） Chain C 1–339（339 aa）	Not recorded	MG MAGNESIUM ION × 3 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；25mM Tris-HCl, pH 7.5, 50mM KCl, 1mM dithiothreitol, 1mM AMP-PNP and 2mM MgCl2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.50 Å
5JZC helical filament Deposited 2016-05-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric	Chain A 1–339（339 aa） Chain B 1–339（339 aa） Chain C 1–339（339 aa） Chain D 1–339（339 aa） Chain E 1–339（339 aa） Chain F 1–339（339 aa） Chain G 1–339（339 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7	Resolution 4.20 Å
5NP7 CryoEM structure of Human Rad51 on single-stranded DNA to 4.2A resolution. Deposited 2017-04-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric	Chain A 1–339（339 aa） Chain B 1–339（339 aa） Chain C 1–339（339 aa） Chain D 1–339（339 aa） Chain E 1–339（339 aa） Chain F 1–339（339 aa） Chain G 1–339（339 aa）	Not recorded	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 4.20 Å
5NWL Crystal structure of a human RAD51-ATP filament. Deposited 2017-05-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric	Chain A 1–339（339 aa） Chain B 1–339（339 aa） Chain C 1–339（339 aa） Chain D 1–339（339 aa） Chain E 1–339（339 aa） Chain F 1–339（339 aa） Chain G 1–339（339 aa）	Not recorded	MG MAGNESIUM ION × 7 ATP ADENOSINE-5'-TRIPHOSPHATE × 7	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1 MES pH 5.2 MPD	Resolution 3.93 Å R-free 0.317
5NWL Crystal structure of a human RAD51-ATP filament. Deposited 2017-05-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric	Chain H 1–339（339 aa） Chain I 1–339（339 aa） Chain J 1–339（339 aa） Chain K 1–339（339 aa） Chain L 1–339（339 aa） Chain M 1–339（339 aa） Chain N 1–339（339 aa）	Not recorded	MG MAGNESIUM ION × 7 ATP ADENOSINE-5'-TRIPHOSPHATE × 7	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1 MES pH 5.2 MPD	Resolution 3.93 Å R-free 0.317
7C9A Human RAD51 post-synaptic complexes mutant (V273P, D274G) Deposited 2020-06-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 3 PDB declaration: pentameric	Chain A 1–339（339 aa） Chain B 1–339（339 aa） Chain C 1–339（339 aa）	Mutation：V273P, D274G Mutation：V273P, D274G Mutation：V273P, D274G	CA CALCIUM ION × 3 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；25 mM Tris-HCl, pH 7.5, 50 mM KCl and 1 mM dithiothreitol) containing 2 mM AMP-PNP and 5 mM CaCl2 cryo-EM vitrification conditions Cryogen ETHANE；The grids were blotted for 1 sec at 22 degree C with 100% relative humidity and plunge-frozen in liquid ethane cooled by liquid nitrogen using a Vitrobot Mark IV (Thermo Fisher).	Resolution 3.43 Å
7EJC human RAD51 presynaptic complex Deposited 2021-04-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 3 PDB declaration: tetrameric	Chain A 1–339（339 aa） Chain B 1–339（339 aa） Chain C 1–339（339 aa）	Not recorded	MG MAGNESIUM ION × 3 J46 4-bromanyl-N-(4-bromophenyl)-3-[(phenylmethyl)sulfamoyl]benzamide × 3 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.97 Å
7EJE human RAD51 post-synaptic complex Deposited 2021-04-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 3 PDB declaration: pentameric	Chain A 1–339（339 aa） Chain B 1–339（339 aa） Chain C 1–339（339 aa）	Not recorded	MG MAGNESIUM ION × 3 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.98 Å
8BQ2 CryoEM structure of the pre-synaptic RAD51 nucleoprotein filament in the presence of ATP and Ca2+ Deposited 2022-11-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 9 PDB declaration: decameric	Chain A 1–339（339 aa） Chain B 1–339（339 aa） Chain C 1–339（339 aa） Chain D 1–339（339 aa） Chain E 1–339（339 aa） Chain F 1–339（339 aa） Chain G 1–339（339 aa） Chain H 1–339（339 aa） Chain I 1–339（339 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 9 CA CALCIUM ION × 18	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
8BR2 CryoEM structure of the post-synaptic RAD51 nucleoprotein filament in the presence of ATP and Ca2+ Deposited 2022-11-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 6 PDB declaration: octameric	Chain A 1–339（339 aa） Chain B 1–339（339 aa） Chain C 1–339（339 aa） Chain D 1–339（339 aa） Chain E 1–339（339 aa） Chain F 1–339（339 aa）	Not recorded	CA CALCIUM ION × 12 ATP ADENOSINE-5'-TRIPHOSPHATE × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.90 Å
8BSC CryoEM structure of the RAD51 nucleoprotein filament in the presence of ADP and Ca2+ Deposited 2022-11-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric	Chain A 1–339（339 aa） Chain B 1–339（339 aa） Chain C 1–339（339 aa） Chain D 1–339（339 aa） Chain E 1–339（339 aa） Chain F 1–339（339 aa） Chain G 1–339（339 aa）	Not recorded	CA CALCIUM ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
8GYK CryoEM structure of the RAD51_ADP filament Deposited 2022-09-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–339（339 aa） Chain B 1–339（339 aa） Chain C 1–339（339 aa） Chain D 1–339（339 aa） Chain E 1–339（339 aa） Chain F 1–339（339 aa） Chain G 1–339（339 aa） Chain H 1–339（339 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 8 MG MAGNESIUM ION × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.14 Å
8JND The cryo-EM structure of the nonameric RAD51 ring bound to the nucleosome with the linker DNA binding Deposited 2023-06-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 17 PDB declaration: 19-meric	Chain K 1–339（339 aa） Chain L 1–339（339 aa） Chain M 1–339（339 aa） Chain N 1–339（339 aa） Chain O 1–339（339 aa） Chain P 1–339（339 aa） Chain Q 1–339（339 aa） Chain R 1–339（339 aa） Chain S 1–339（339 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.66 Å
8JNE The cryo-EM structure of the decameric RAD51 ring bound to the nucleosome without the linker DNA binding Deposited 2023-06-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 18 PDB declaration: 20-meric	Chain K 1–339（339 aa） Chain L 1–339（339 aa） Chain M 1–339（339 aa） Chain N 1–339（339 aa） Chain O 1–339（339 aa） Chain P 1–339（339 aa） Chain Q 1–339（339 aa） Chain R 1–339（339 aa） Chain S 1–339（339 aa） Chain T 1–339（339 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.68 Å
8JNF The cryo-EM structure of the RAD51 filament bound to the nucleosome Deposited 2023-06-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 14 PDB declaration: 16-meric	Chain K 1–339（339 aa） Chain L 1–339（339 aa） Chain M 1–339（339 aa） Chain N 1–339（339 aa） Chain O 1–339（339 aa） Chain P 1–339（339 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.91 Å
8PBC RAD51 filament on ssDNA bound by the BRCA2 c-terminus Deposited 2023-06-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 21 PDB declaration: 22-meric	Chain A 1–339（339 aa） Chain B 1–339（339 aa） Chain C 1–339（339 aa） Chain D 1–339（339 aa） Chain E 1–339（339 aa） Chain F 1–339（339 aa） Chain G 1–339（339 aa） Chain H 1–339（339 aa） Chain I 1–339（339 aa） Chain J 1–339（339 aa） Chain K 1–339（339 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 11 CA CALCIUM ION × 22	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.61 Å
8PBD RAD51 filament on dsDNA bound by the BRCA2 c-terminus Deposited 2023-06-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 19 PDB declaration: 21-meric	Chain A 1–339（339 aa） Chain B 1–339（339 aa） Chain C 1–339（339 aa） Chain D 1–339（339 aa） Chain E 1–339（339 aa） Chain F 1–339（339 aa） Chain G 1–339（339 aa） Chain H 1–339（339 aa） Chain I 1–339（339 aa） Chain J 1–339（339 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 10 CA CALCIUM ION × 20	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.83 Å
8R64 Cryo-EM structure of the FIGNL1 AAA hexamer bound to RAD51 Deposited 2023-11-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain G 1–339（339 aa）	Not recorded	MG MAGNESIUM ION × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
8RCD RAD51 nucleoprotein filament on abasic single-stranded DNA Deposited 2023-12-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 8 PDB declaration: nonameric	Chain A 1–339（339 aa） Chain B 1–339（339 aa） Chain C 1–339（339 aa） Chain D 1–339（339 aa） Chain E 1–339（339 aa） Chain F 1–339（339 aa） Chain G 1–339（339 aa） Chain H 1–339（339 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 8 CA CALCIUM ION × 16	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
8RCF RAD51 nucleoprotein filament on double-stranded abasic DNA Deposited 2023-12-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 8 PDB declaration: decameric	Chain A 1–339（339 aa） Chain B 1–339（339 aa） Chain C 1–339（339 aa） Chain D 1–339（339 aa） Chain E 1–339（339 aa） Chain F 1–339（339 aa） Chain G 1–339（339 aa） Chain H 1–339（339 aa）	Not recorded	CA CALCIUM ION × 16 ATP ADENOSINE-5'-TRIPHOSPHATE × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
8UVW Crystal structure of RAD51-BRCA2 Cter complex Deposited 2023-11-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 85–339（255 aa） Chain D 97–339（243 aa）	Mutation：C319S Mutation：S208E,A209D,C3287A,C3304A,C391S	ADP ADENOSINE-5'-DIPHOSPHATE × 2 BEF BERYLLIUM TRIFLUORIDE ION × 2 EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；25% v/v 1,4-Dioxane 0.05 M MOPS pH 7.0 0.005 M Magnesium chloride hexahydrate 0.001 M Spermine	Resolution 2.73 Å R-free 0.282
8XBT The cryo-EM structure of the octameric RAD51 ring bound to the nucleosome with the linker DNA binding Deposited 2023-12-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 16 PDB declaration: 18-meric	Chain K 1–339（339 aa） Chain L 1–339（339 aa） Chain M 1–339（339 aa） Chain N 1–339（339 aa） Chain O 1–339（339 aa） Chain P 1–339（339 aa） Chain Q 1–339（339 aa） Chain R 1–339（339 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.12 Å
8XBU The cryo-EM structure of the decameric RAD51 ring bound to the nucleosome with the linker DNA binding Deposited 2023-12-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 18 PDB declaration: 20-meric	Chain K 1–339（339 aa） Chain L 1–339（339 aa） Chain M 1–339（339 aa） Chain N 1–339（339 aa） Chain O 1–339（339 aa） Chain P 1–339（339 aa） Chain Q 1–339（339 aa） Chain R 1–339（339 aa） Chain S 1–339（339 aa） Chain T 1–339（339 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.24 Å
8XBV The cryo-EM structure of the RAD51 L1 and L2 loops bound to the linker DNA with the sticky end of the nucleosome Deposited 2023-12-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric	Chain K 1–339（339 aa） Chain L 1–339（339 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 7.61 Å
8XBW The cryo-EM structure of the RAD51 N-terminal lobe domain bound to the histone H4 tail of the nucleosome Deposited 2023-12-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 3 PDB declaration: pentameric	Chain L 1–339（339 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.89 Å
8XBX The cryo-EM structure of the RAD51 L2 loop bound to the linker DNA with the blunt end of the nucleosome Deposited 2023-12-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 3 PDB declaration: pentameric	Chain K 1–339（339 aa） Chain L 1–339（339 aa） Chain M 1–339（339 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.36 Å
8XBY The cryo-EM structure of the RAD51 L1 and L2 loops bound to the linker DNA with the blunt end of the nucleosome Deposited 2023-12-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 3 PDB declaration: pentameric	Chain K 1–339（339 aa） Chain L 1–339（339 aa） Chain M 1–339（339 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 7.80 Å
9I62 CryoEM structure of a RAD51 D-loop Deposited 2025-01-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 9 PDB declaration: 12-meric	Chain A 1–339（339 aa） Chain B 1–339（339 aa） Chain C 1–339（339 aa） Chain D 1–339（339 aa） Chain E 1–339（339 aa） Chain F 1–339（339 aa） Chain G 1–339（339 aa） Chain H 1–339（339 aa） Chain I 1–339（339 aa）	Not recorded	CA CALCIUM ION × 18 ATP ADENOSINE-5'-TRIPHOSPHATE × 9	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.64 Å
9OMY Cryo-EM structure of an octameric RAD51-XRCC3-RAD51C (RAD51-X3C) complex Deposited 2025-05-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–339（339 aa） Chain B 1–339（339 aa） Chain D 1–339（339 aa） Chain E 1–339（339 aa）	Not recorded	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.25 Å
9OMZ Cryo-EM structure of a pentameric RAD51-XRCC3-RAD51C-RAD51D-XRCC2 (51-X3CDX2) complex. Deposited 2025-05-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 1–339（339 aa）	Not recorded	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.51 Å
9Q23 DX2-CX3-RAD51 structure in the intermediate state Deposited 2025-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 6 PDB declaration: heptameric	Chain G 1–339（339 aa） Chain I 1–339（339 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.84 Å
9Q25 DX2-CX3-RAD51 in the closed state Deposited 2025-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 5 PDB declaration: hexameric	Chain G 1–339（339 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.24 Å
9Q28 DX2-CX3-RAD51 in the active state Deposited 2025-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 6 PDB declaration: heptameric	Chain G 1–339（339 aa） Chain I 1–339（339 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.84 Å
9Q29 DX2-CX3 structure capping RAD51 filament Deposited 2025-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 9 PDB declaration: decameric	Chain G 1–339（339 aa） Chain I 1–339（339 aa） Chain J 1–339（339 aa） Chain K 1–339（339 aa） Chain L 1–339（339 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 1 CA CALCIUM ION × 13 ATP ADENOSINE-5'-TRIPHOSPHATE × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.61 Å
9Q2A BCDX2-CX3-RAD51-RAD51-ssDNA supercomplex Deposited 2025-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 8 PDB declaration: nonameric	Chain G 1–339（339 aa） Chain I 1–339（339 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.67 Å
9Q2B DX2-CX3-RAD51 bound to DNA bubble Deposited 2025-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 6 PDB declaration: octameric	Chain G 1–339（339 aa） Chain I 1–339（339 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
9QN8 RAD51 filament in complex with calcium and ATP bound by the RAD51AP1 C-terminus Deposited 2025-03-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 12 PDB declaration: 13-meric	Chain A 1–339（339 aa） Chain C 1–339（339 aa） Chain E 1–339（339 aa） Chain G 1–339（339 aa） Chain I 1–339（339 aa） Chain K 1–339（339 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 7 CA CALCIUM ION × 7 K POTASSIUM ION × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.14 Å
9QNA RAD51 filament in complex with magnesium and ATP Deposited 2025-03-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 6 PDB declaration: heptameric	Chain A 1–339（339 aa） Chain C 1–339（339 aa） Chain E 1–339（339 aa） Chain G 1–339（339 aa） Chain I 1–339（339 aa） Chain K 1–339（339 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 7 MG MAGNESIUM ION × 6 K POTASSIUM ION × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.26 Å
9QNB RAD51 filament in complex with magnesium and ADP Deposited 2025-03-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–339（339 aa） Chain C 1–339（339 aa） Chain E 1–339（339 aa） Chain G 1–339（339 aa） Chain I 1–339（339 aa） Chain K 1–339（339 aa）	Not recorded	MG MAGNESIUM ION × 6 ADP ADENOSINE-5'-DIPHOSPHATE × 6 K POTASSIUM ION × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.63 Å
9QNC RAD51 filament in complex with magnesium and ATP bound by the RAD51AP1 C-terminus Deposited 2025-03-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 12 PDB declaration: 13-meric	Chain A 1–339（339 aa） Chain C 1–339（339 aa） Chain E 1–339（339 aa） Chain G 1–339（339 aa） Chain I 1–339（339 aa） Chain K 1–339（339 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 7 K POTASSIUM ION × 5 MG MAGNESIUM ION × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.98 Å
9SRZ RAD51-ssDNA filament in complex with calcium and ATP bound by the RAD54B N-terminus Deposited 2025-09-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 12 PDB declaration: 13-meric	Chain I 1–339（339 aa） Chain J 1–339（339 aa） Chain K 1–339（339 aa） Chain L 1–339（339 aa） Chain M 1–339（339 aa） Chain N 1–339（339 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 6 CA CALCIUM ION × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.61 Å
9SSL RAD51-ssDNA filament in complex with magnesium and ATP bound by the RAD54B N-terminus (peptide) Deposited 2025-09-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 12 PDB declaration: 13-meric	Chain A 1–339（339 aa） Chain B 1–339（339 aa） Chain C 1–339（339 aa） Chain D 1–339（339 aa） Chain E 1–339（339 aa） Chain F 1–339（339 aa）	Not recorded	K POTASSIUM ION × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 7 MG MAGNESIUM ION × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.90 Å
9SVX XRCC3-RAD51C-RAD51D-XRCC2 (XRCC3 complex) capping a RAD51 filament on single stranded DNA Deposited 2025-10-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 9 PDB declaration: decameric	Chain E 1–339（339 aa） Chain F 1–339（339 aa） Chain G 1–339（339 aa） Chain H 1–339（339 aa） Chain I 1–339（339 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 7 CA CALCIUM ION × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；25 mM HEPES-NaOH pH 7.5, 100 mM NaCl, 2.5 mM MgCl2, 2.5 mM CaCl2, 1 mM ATP, 0.25 mM TCEP cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.70 Å
9SVY XRCC3-RAD51C-RAD51D-XRCC2 (XRCC3 complex) capping a RAD51 filament on partially duplex DNA Deposited 2025-10-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 11 PDB declaration: 13-meric	Chain E 1–339（339 aa） Chain F 1–339（339 aa） Chain G 1–339（339 aa） Chain H 1–339（339 aa） Chain I 1–339（339 aa） Chain J 1–339（339 aa） Chain K 1–339（339 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 9 MG MAGNESIUM ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 1 CA CALCIUM ION × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；25 mM HEPES-NaOH pH 7.5, 100 mM NaCl, 2.5 mM MgCl2, 2.5 mM CaCl2, 1 mM ATP, 0.25 mM TCEP cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.60 Å
9SW0 XRCC3-RAD51C-RAD51D-XRCC2 (XRCC3 complex) capping a RAD51 filament on a D-loop intermediate Deposited 2025-10-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 11 PDB declaration: 14-meric	Chain E 1–339（339 aa） Chain F 1–339（339 aa） Chain G 1–339（339 aa） Chain H 1–339（339 aa） Chain I 1–339（339 aa） Chain J 1–339（339 aa） Chain K 1–339（339 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 8 CA CALCIUM ION × 7 MG MAGNESIUM ION × 8 ADP ADENOSINE-5'-DIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；25 mM HEPES-NaOH pH 7.5, 100 mM NaCl, 2.5 mM MgCl2, 2.5 mM CaCl2, 1 mM ATP, 0.25 mM TCEP cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
9TRL RAD51-ssDNA filament in complex with magnesium and ATP bound by the RAD54B N-terminus (beta-barrel) Deposited 2025-12-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 11 PDB declaration: 12-meric	Chain A 1–339（339 aa） Chain B 1–339（339 aa） Chain C 1–339（339 aa） Chain D 1–339（339 aa） Chain E 1–339（339 aa） Chain F 1–339（339 aa）	Not recorded	K POTASSIUM ION × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 7 MG MAGNESIUM ION × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
9TRM RAD51-dsDNA filament in complex with calcium and ATP bound by the RAD54B N-terminus Deposited 2025-12-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 13 PDB declaration: 15-meric	Chain I 1–339（339 aa） Chain J 1–339（339 aa） Chain K 1–339（339 aa） Chain L 1–339（339 aa） Chain M 1–339（339 aa） Chain N 1–339（339 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 6 CA CALCIUM ION × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.40 Å
9TYY RAD51-ssDNA filament in complex with calcium and ATP bound by the RAD54 N-terminus Deposited 2026-01-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 12 PDB declaration: 13-meric	Chain I 1–339（339 aa） Chain J 1–339（339 aa） Chain K 1–339（339 aa） Chain L 1–339（339 aa） Chain M 1–339（339 aa） Chain N 1–339（339 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 6 CA CALCIUM ION × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
9ZZR Cryo-EM Structure of a RAD51 filament bound by ssDNA and the XRCC3-RAD51C-RAD51D-XRCC2 paralog complex Deposited 2026-01-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 11 PDB declaration: dodecameric	Chain E 22–338（317 aa） Chain F 24–337（314 aa） Chain K 22–338（317 aa） Chain O 22–338（317 aa） Chain R 22–337（316 aa） Chain V 22–337（316 aa） Chain W 22–338（317 aa）	Not recorded	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 11	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.95 Å

50 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	RAD51_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–243； UniProt 97–339

Breast cancer type 2 susceptibility protein

Homo sapiens

UniProt P51587

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain B； UniProt 1517–1551	Fragment：BRC repeat type 4	DNA repair protein RAD51 homolog 1 × 1 （Q06609） peptide linker × 1 ARTIFICIAL GLY-SER-MSE-GLY PEPTIDE × 1 MG MAGNESIUM ION × 1 CL CHLORIDE ION × 1 EDO 1,2-ETHANEDIOL × 5	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.2；291 K；ETHYLENE GLYCOL, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 1.70 Å R-free 0.206

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 1N0W	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3EU7 Crystal Structure of a PALB2 / BRCA2 complex Deposited 2008-10-09	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain X 21–39（19 aa） Fragment：Interaction with PALB2, residues 21-39	Not recorded	GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；0.1M Na-Cacodylate pH 6.5, 0.2M magnesium acetate, 10% (w/v) PEG 8000, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.20 Å R-free 0.253
7BDX Armadillo domain of HSF2BP in complex with BRCA2 peptide Deposited 2020-12-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain E 2291–2343（53 aa） Chain F 2291–2343（53 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；293 K；PEG 3350 : 16% (w/v) Mes ph 6.0 100 mM MgCl2 100 mM	Resolution 2.60 Å R-free 0.241
7LDG Crystal structure of the MEILB2-BRCA2 complex Deposited 2021-01-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain B 2271–2335（65 aa） Fragment：MEILB2-binding domain (aa2271-2335) Chain D 2271–2335（65 aa） Fragment：MEILB2-binding domain (aa2271-2335)	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；289 K；0.1 M sodium acetate (pH 4.6), 2 M lithium acetate	Resolution 2.56 Å R-free 0.231
8BR9 Stapled peptide SP24 in complex with humanised RadA mutant HumRadA22 Deposited 2022-11-22	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1226–1263（38 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 1 RF6 4,6-diethylpyrimidin-2-amine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291.15 K；0.1 M Na 3 Cit 4.2 pH (Buffer) 20 %w/v PEG 1K (Precipitant) 0.2 M Li 2 SO4 (Salt)	Resolution 1.63 Å R-free 0.282
8C3J Stapled peptide SP2 in complex with humanised RadA mutant HumRadA22 Deposited 2022-12-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1226–1244（19 aa） Chain C 2050–2064（15 aa）	Not recorded	TKI 2-[(4,6-diethyl-1,3,5-triazin-2-yl)-methyl-amino]ethanoic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein in 20 mM CHES pH 9.5, 100 mM NaCl. Condition: 8 % w/v PEG 8000 (precipitant) 0.08 M Potassium phosphate pH 5.6 (buffer) 200:200 uL drop	Resolution 3.02 Å R-free 0.281
8C3J Stapled peptide SP2 in complex with humanised RadA mutant HumRadA22 Deposited 2022-12-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain J 1226–1244（19 aa） Chain J 2050–2064（15 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein in 20 mM CHES pH 9.5, 100 mM NaCl. Condition: 8 % w/v PEG 8000 (precipitant) 0.08 M Potassium phosphate pH 5.6 (buffer) 200:200 uL drop	Resolution 3.02 Å R-free 0.281
8C3N Stapled peptide SP30 in complex with humanised RadA mutant HumRadA22 Deposited 2022-12-27	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1215–1243（29 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 RF6 4,6-diethylpyrimidin-2-amine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein: 0.5 mM SP30:HumRadA22 in 20 mM CHES pH 9.5, 100 mM NaCl, 20 mM ADP/MgCl 2 Condition: 14% w/v PEG 4000 (precipitant), 6% v/v MPD (precipitant), 0.1M Na K Phos pH 6.2 (buffer)	Resolution 1.21 Å R-free 0.218
8PBC RAD51 filament on ssDNA bound by the BRCA2 c-terminus Deposited 2023-06-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 21 PDB declaration: 22-meric	Chain L 3260–3308（49 aa） Chain M 3260–3308（49 aa） Chain N 3260–3308（49 aa） Chain O 3260–3308（49 aa） Chain P 3260–3308（49 aa） Chain Q 3260–3308（49 aa） Chain R 3260–3308（49 aa） Chain S 3260–3308（49 aa） Chain T 3260–3308（49 aa） Chain U 3260–3308（49 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 11 CA CALCIUM ION × 22	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.61 Å
8PBD RAD51 filament on dsDNA bound by the BRCA2 c-terminus Deposited 2023-06-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 19 PDB declaration: 21-meric	Chain K 3260–3308（49 aa） Chain L 3260–3308（49 aa） Chain M 3260–3308（49 aa） Chain N 3260–3308（49 aa） Chain O 3260–3308（49 aa） Chain P 3260–3308（49 aa） Chain Q 3260–3308（49 aa） Chain R 3260–3308（49 aa） Chain S 3260–3308（49 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 10 CA CALCIUM ION × 20	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.83 Å
8QQE Crystal structure of the complex between DMC1 and the PhePP domain of BRCA2 Deposited 2023-10-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric	Chain C 2398–2417（20 aa） Chain D 2398–2417（20 aa）	Not recorded	MG MAGNESIUM ION × 4 CL CHLORIDE ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6；293 K；0.1M MES at pH 6, 2.4 M sodium formate	Resolution 3.46 Å R-free 0.261
8R2G Crystal structure of a BRCA2-DMC1 complex Deposited 2023-11-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 15 PDB declaration: pentadecameric	Chain I 2400–2413（14 aa） Chain J 2400–2413（14 aa） Chain K 2400–2413（14 aa） Chain L 2400–2413（14 aa） Chain M 2400–2413（14 aa） Chain N 2400–2413（14 aa） Chain O 2400–2413（14 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；50 mM HEPES-NaOH pH 7.4, 50 mM MgCl2, 500 mM NaCl, 8 % PEG 3350, 20 % glycerol	Resolution 3.45 Å R-free 0.306
8UVW Crystal structure of RAD51-BRCA2 Cter complex Deposited 2023-11-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 1517–1547（31 aa） Chain D 3270–3305（36 aa）	Mutation：C319S Mutation：S208E,A209D,C3287A,C3304A,C391S	ADP ADENOSINE-5'-DIPHOSPHATE × 2 BEF BERYLLIUM TRIFLUORIDE ION × 2 EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；25% v/v 1,4-Dioxane 0.05 M MOPS pH 7.0 0.005 M Magnesium chloride hexahydrate 0.001 M Spermine	Resolution 2.73 Å R-free 0.282

11 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	BRCA2_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–35； UniProt 1517–1551

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.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1n0w
Deposition date deposition_date	2002-10-15
Structure title title	Crystal structure of a RAD51-BRCA2 BRC repeat complex
Keywords keywords	;DNA repair, homologous recombination, breast cancer susceptibility, RecA-like ATPase, protein complex, GENE REGULATION-ANTITUMOR PROTEIN COMPLEX ;; GENE REGULATION/ANTITUMOR PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	19.47 Å
Radius of gyration Rg (electron density) rg_electron	18.15 Å
Forward intensity I(0) i0	15174900.00
Molecular weight molecular_weight	28148.0 kDa
Excluded volume excluded_volume	34764 Å³
Envelope volume envelope_volume	41982 Å³
Hydration-shell volume shell_volume	19068 Å³
Envelope diameter envelope_diameter	70.0 Å
Shell Rg shell_rg	24.94 Å
Envelope Rg envelope_rg	19.16 Å
Shape Rg shape_rg	18.10 Å
Total Rg total_rg	19.30 Å
Total atoms total_atoms	1941
Residues n_residues	242
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	70.0 Å
Rg (real space) rg_real	19.43 Å
Rg uncertainty (real space) rg_real_error	0.54 Å
I(0) (real space) i0_real	1.5170e+07
I(0) uncertainty (real space) i0_real_error	1.9220e+05
Rg (reciprocal space) rg_reciprocal	19.43 Å
I(0) (reciprocal space) i0_reciprocal	15170000.0000
Solution quality estimate total_estimate	0.8343
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	23.7 Å
Skewness Skewness skewness	0.372
Kurtosis Kurtosis kurtosis	0.023
Angular range angular_range	— – 0.4100 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	4292000.0000
Real-space data points n_real_points	72
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.631; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.955; Smooth: 0.996

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (8)

Entity 1 Entity 1 polymer

Description description	DNA repair protein RAD51 homolog 1
Molecular weight formula_weight	26855.3 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2225

SEIIQITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPERLLAVAERYGLSGSDVLDNVAYARAFNTDHQTQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLRMLLRLADEFGVAVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPCLPEAEAMFAINADGVGDAKD

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 polymer

Description description	Breast cancer type 2 susceptibility protein
Molecular weight formula_weight	3966.6 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

KEPTLLGFHTASGKKVKIAKESLDKVKNLFDEKEQ

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli BL21(DE3)

Entity 3 Entity 3 polymer

Description description	peptide linker
Molecular weight formula_weight	1234.1 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	L

TGSTGSTGSTGSMG

来源 Source

宿主生物 host_organism

Escherichia coli BL21(DE3)

Entity 4 Entity 4 polymer

Description description	ARTIFICIAL GLY-SER-MSE-GLY PEPTIDE
Molecular weight formula_weight	397.3 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

GSMG

来源 Source

宿主生物 host_organism

Escherichia coli BL21(DE3)

Entity 5 Entity 5 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 6 Entity 6 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 7 Entity 7 non-polymer

Description description	1,2-ETHANEDIOL
Molecular weight formula_weight	62.1 kDa
Source method src_method	syn
Copy count entity_count	5

Entity 8 Entity 8 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	247

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1n0wa_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.11 — RecA protein-like (ATPase-domain)

Domain ID domain_id	d1n0wb_
Class class	j — Peptides
Fold Fold fold	j.97 — BRCA2 BRC4 repeat
Superfamily Superfamily superfamily	j.97.1 — BRCA2 BRC4 repeat
Family Family family	j.97.1.1 — BRCA2 BRC4 repeat

CATH v4.4 (1 domains)

Domain ID domain_id	1n0wA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

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8. Citations (1)

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Unit-cell length a length_a	57.300 Å
Unit-cell length b length_b	59.140 Å
Unit-cell length c length_c	77.200 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	4

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

Resolution resolution	1.700 Å
Low-resolution limit resolution_low	24.850 Å
R factor r_factor	—
R_work r_work	0.1910
R_free r_free	0.2060

fit	/app/data/saxs_computation/n0/1n0w/1n0w.fit
pddf	/app/data/pr_computation/n0/1n0w/1n0w.pr.out
profile	/app/data/saxs_computation/n0/1n0w/1n0w.dat

Crystal structure of a RAD51-BRCA2 BRC repeat complex

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

DNA repair protein RAD51 homolog 1

State in the Current Structure

Other States of the Same Protein in the Database

Breast cancer type 2 susceptibility protein

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (8)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

Entity 4 Entity 4 polymer

Polymer Polymer

来源 Source

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 non-polymer

Entity 8 Entity 8 water

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)