SAXSdb — 8r2g

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

Meiotic recombination protein DMC1/LIM15 homolog

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 × 15 PDB declaration: pentadecameric（15） Consistent with protein copy count	Chain A； UniProt 83–340 Chain B； UniProt 83–340 Chain C； UniProt 83–340 Chain D； UniProt 83–340 Chain E； UniProt 83–340 Chain F； UniProt 83–340 Chain G； UniProt 83–340 Chain H； UniProt 83–340	Not recorded	Breast cancer type 2 susceptibility protein × 7 （P51587）	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

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 8R2G	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1V5W Crystal structure of the human Dmc1 protein Deposited 2003-11-26	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–340（340 aa） Chain B 1–340（340 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.8；293 K；PEG2000MME, Magnesium chloride, Sodium citrate, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.20 Å R-free 0.346
1V5W Crystal structure of the human Dmc1 protein Deposited 2003-11-26	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 16 PDB declaration: hexadecameric	Chain A 1–340（340 aa） Chain B 1–340（340 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.8；293 K；PEG2000MME, Magnesium chloride, Sodium citrate, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.20 Å R-free 0.346
2ZJB Crystal structure of the human Dmc1-M200V polymorphic variant Deposited 2008-03-02	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–340（340 aa） Chain B 1–340（340 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.8；293 K；0.1M sodium citrate, 50mM MgCl2, 8% PEG 2000 MME, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.50 Å R-free 0.351
4HYY Filament of octameric rings of DMC1 recombinase from Homo sapiens Deposited 2012-11-14	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 84–340（257 aa） Fragment：ATPase domain Chain B 84–340（257 aa） Fragment：ATPase domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；294 K；6% PEG 3350, 0.5 M NaCl, 0.05 M MgCl2, 0.05 M HEPES-NACl, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 294.0K	Resolution 2.60 Å R-free 0.246
4HYY Filament of octameric rings of DMC1 recombinase from Homo sapiens Deposited 2012-11-14	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain C 84–340（257 aa） Fragment：ATPase domain Chain D 84–340（257 aa） Fragment：ATPase domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；294 K；6% PEG 3350, 0.5 M NaCl, 0.05 M MgCl2, 0.05 M HEPES-NACl, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 294.0K	Resolution 2.60 Å R-free 0.246
4HYY Filament of octameric rings of DMC1 recombinase from Homo sapiens Deposited 2012-11-14	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 16 PDB declaration: hexadecameric	Chain A 84–340（257 aa） Fragment：ATPase domain Chain B 84–340（257 aa） Fragment：ATPase domain Chain C 84–340（257 aa） Fragment：ATPase domain Chain D 84–340（257 aa） Fragment：ATPase domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；294 K；6% PEG 3350, 0.5 M NaCl, 0.05 M MgCl2, 0.05 M HEPES-NACl, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 294.0K	Resolution 2.60 Å R-free 0.246
6R3P Crystal structure of human DMC1 ATPase domain Deposited 2019-03-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 83–340（258 aa） Chain B 83–340（258 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.2；293 K；50 mM HEPES-NaOH pH 7.2, 50 mM MgCl2, 500 mM NaCl, 7.5 % PEG3350	Resolution 2.05 Å R-free 0.219
6R3P Crystal structure of human DMC1 ATPase domain Deposited 2019-03-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain C 83–340（258 aa） Chain D 83–340（258 aa）	Not recorded	PEG DI(HYDROXYETHYL)ETHER × 8 PG4 TETRAETHYLENE GLYCOL × 4 P6G HEXAETHYLENE GLYCOL × 8 1PE PENTAETHYLENE GLYCOL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.2；293 K；50 mM HEPES-NaOH pH 7.2, 50 mM MgCl2, 500 mM NaCl, 7.5 % PEG3350	Resolution 2.05 Å R-free 0.219
7C98 Human DMC1 post-synaptic complexes 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 1–340（340 aa） Chain B 1–340（340 aa） Chain C 1–340（340 aa）	Not recorded	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 3.47 Å
7C99 Human DMC1 post-synaptic complexes with mismatched dsDNA 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 1–340（340 aa） Chain B 1–340（340 aa） Chain C 1–340（340 aa）	Not recorded	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 3.36 Å
7C9C Human DMC1 pre-synaptic complexes 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: tetrameric	Chain A 1–340（340 aa） Chain B 1–340（340 aa） Chain C 1–340（340 aa）	Not recorded	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 3.33 Å
7CGY Human DMC1 Q244M mutant of the post-synaptic complexes Deposited 2020-07-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–340（340 aa） Chain B 1–340（340 aa） Chain C 1–340（340 aa）	Mutation：Q244M Mutation：Q244M Mutation：Q244M	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 3.20 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 A 2–340（339 aa） Chain B 2–340（339 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

9 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	DMC1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–261； UniProt 83–340 Author chain B； PDBConstruct 4–261； UniProt 83–340 Author chain C； PDBConstruct 4–261； UniProt 83–340 Author chain D； PDBConstruct 4–261； UniProt 83–340 Author chain E； PDBConstruct 4–261； UniProt 83–340 Author chain F； PDBConstruct 4–261； UniProt 83–340 Author chain G； PDBConstruct 4–261； UniProt 83–340 Author chain H； PDBConstruct 4–261； UniProt 83–340

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 × 15 PDB declaration: pentadecameric（15） Consistent with protein copy count	Chain I； UniProt 2400–2413 Chain J； UniProt 2400–2413 Chain K； UniProt 2400–2413 Chain L； UniProt 2400–2413 Chain M； UniProt 2400–2413 Chain N； UniProt 2400–2413 Chain O； UniProt 2400–2413	Not recorded	Meiotic recombination protein DMC1/LIM15 homolog × 8 （Q14565）	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

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 8R2G	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1N0W Crystal structure of a RAD51-BRCA2 BRC repeat complex Deposited 2002-10-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 1517–1551（35 aa） Fragment：BRC repeat type 4	Not recorded	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
3EU7 Crystal Structure of a PALB2 / BRCA2 complex Deposited 2008-10-09	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 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 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 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 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 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 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 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
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 I； PDBConstruct 1–14； UniProt 2400–2413 Author chain J； PDBConstruct 1–14； UniProt 2400–2413 Author chain K； PDBConstruct 1–14； UniProt 2400–2413 Author chain L； PDBConstruct 1–14； UniProt 2400–2413 Author chain M； PDBConstruct 1–14； UniProt 2400–2413 Author chain N； PDBConstruct 1–14； UniProt 2400–2413 Author chain O； PDBConstruct 1–14； UniProt 2400–2413

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	8r2g
Deposition date deposition_date	2023-11-05
Structure title title	Crystal structure of a BRCA2-DMC1 complex
Keywords keywords	DNA repair, recombination, meiosis; RECOMBINATION
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	47.46 Å
Radius of gyration Rg (electron density) rg_electron	46.95 Å
Forward intensity I(0) i0	666815000.00
Molecular weight molecular_weight	217820.0 kDa
Excluded volume excluded_volume	273550 Å³
Envelope volume envelope_volume	384010 Å³
Hydration-shell volume shell_volume	64120 Å³
Envelope diameter envelope_diameter	145.0 Å
Shell Rg shell_rg	57.26 Å
Envelope Rg envelope_rg	45.26 Å
Shape Rg shape_rg	46.99 Å
Total Rg total_rg	47.15 Å
Total atoms total_atoms	15352
Residues n_residues	1958
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	139.9 Å
Rg (real space) rg_real	47.24 Å
Rg uncertainty (real space) rg_real_error	1.10 Å
I(0) (real space) i0_real	6.6680e+08
I(0) uncertainty (real space) i0_real_error	1.0800e+07
Rg (reciprocal space) rg_reciprocal	47.46 Å
I(0) (reciprocal space) i0_reciprocal	667000000.0000
Solution quality estimate total_estimate	0.8678
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	76.3 Å
Skewness Skewness skewness	-0.008
Kurtosis Kurtosis kurtosis	-0.905
Angular range angular_range	— – 0.1650 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	108700000.0000
Real-space data points n_real_points	34
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.949; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.433

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	Meiotic recombination protein DMC1/LIM15 homolog
Molecular weight formula_weight	28868.8 kDa
Source method src_method	man
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H
Atom count atom_count	15352

GSMPGFLTAFEYSEKRKMVFHITTGSQEFDKLLGGGIESMAITEAFGEFRTGKTQLSHTLCVTAQLPGAGGYPGGKIIFIDTENTFRPDRLRDIADRFNVDHDAVLDNVLYARAYTSEHQMELLDYVAAKFHEEAGIFKLLIIDSIMALFRVDFSGRGELAERQQKLAQMLSRLQKISEEYNVAVFVTNQMTADPGATMTFQADPKKPIGGHILAHASTTRISLRKGRGELRIAKIYDSPEMPENEATFAITAGGIGDAKE

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

Entity 2 Entity 2 polymer

Description description	Breast cancer type 2 susceptibility protein
Molecular weight formula_weight	1606.0 kDa
Source method src_method	man
Copy count entity_count	7

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	I,J,K,L,M,N,O

GRPTKVFVPPFKTK

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

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8. Citations (1)

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Unit-cell length a length_a	125.400 Å
Unit-cell length b length_b	125.400 Å
Unit-cell length c length_c	364.195 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	64

Space group space_group	P 41 2 2
Space-group number int_tables_number	91
Crystal system crystal_system	tetragonal

Resolution resolution	3.450 Å
Low-resolution limit resolution_low	118.570 Å
R factor r_factor	0.2655
R_work r_work	0.2635
R_free r_free	0.3057

fit	/app/data/saxs_computation/r2/8r2g/8r2g.fit
pddf	/app/data/pr_computation/r2/8r2g/8r2g.pr.out
profile	/app/data/saxs_computation/r2/8r2g/8r2g.dat

Crystal structure of a BRCA2-DMC1 complex

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

Meiotic recombination protein DMC1/LIM15 homolog

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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)