1pzn

Rad51 (RadA)

Method: X-RAY DIFFRACTION D_max: 127.4 Å Quality: GOOD

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

DNA repair and recombination protein rad51

Pyrococcus furiosus

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 homooligomer Homooligomer Protein × 14 PDB declaration: tetradecameric（14） Consistent with protein copy count	Chain A； UniProt 1–349 Chain B； UniProt 1–349 Chain C； UniProt 1–349 Chain D； UniProt 1–349 Chain E； UniProt 1–349 Chain F； UniProt 1–349 Chain G； UniProt 1–349	Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 14 IMD IMIDAZOLE × 18 GOL GLYCEROL × 18 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 8	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.85 Å R-free 0.307
2	Protein homooligomer Homooligomer Protein × 7 PDB declaration: heptameric（7） Consistent with protein copy count	Chain A； UniProt 1–349 Chain B； UniProt 1–349 Chain C； UniProt 1–349 Chain D； UniProt 1–349 Chain E； UniProt 1–349 Chain F； UniProt 1–349 Chain G； UniProt 1–349	Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 7 IMD IMIDAZOLE × 9 GOL GLYCEROL × 9 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.85 Å R-free 0.307

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 1PZN	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
4A6P RadA C-terminal ATPase domain from Pyrococcus furiosus Deposited 2011-11-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa） Fragment：C-TERMINAL ATPASE DOMAIN, RESIDUES 108-288 AND 301-349	Not recorded	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.8；60 MM NA2HPO4 PH 6.0; 15% PEG 1000	Resolution 1.50 Å R-free 0.214
4A6X RadA C-terminal ATPase domain from Pyrococcus furiosus bound to ATP Deposited 2011-11-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa） Fragment：RADA C-TERMINAL ATPASE DOMAIN, RESIDUES 108-349	Not recorded	MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.8；60MM NA2HPO4 PH 6.0; 15% PEG1000	Resolution 1.55 Å R-free 0.235
4A6X RadA C-terminal ATPase domain from Pyrococcus furiosus bound to ATP Deposited 2011-11-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 108–349（242 aa） Fragment：RADA C-TERMINAL ATPASE DOMAIN, RESIDUES 108-349	Not recorded	MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.8；60MM NA2HPO4 PH 6.0; 15% PEG1000	Resolution 1.55 Å R-free 0.235
4B2I Humanised monomeric RadA in complex with indazole Deposited 2012-07-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa） Fragment：ATPASE, RESIDUES 108-349	Mutation：YES	PO4 PHOSPHATE ION × 1 LZ1 1H-indazole × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.2；10-15% PEG-1000, 50 MM NAKPHOSPHATE, PH 6.2	Resolution 1.30 Å R-free 0.223
4B2L Humanised monomeric RadA in complex with L-methylester tryptophan Deposited 2012-07-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa） Fragment：ATPASE, RESIDUES 108-349	Mutation：YES	PO4 PHOSPHATE ION × 1 TR7 methyl L-tryptophanate × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.2；10-15% PEG-1000, 50 MM NAKPHOSPHATE PH 6.2	Resolution 1.50 Å R-free 0.223
4B2P RadA C-terminal ATPase domain from Pyrococcus furiosus bound to GTP Deposited 2012-07-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa） Fragment：C-TERMINAL ATPASE DOMAIN, RESIDUES 108-349	Mutation：YES	GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.2；pH 6.2	Resolution 1.60 Å R-free 0.220
4B32 Humanised monomeric RadA in complex with napht-1-ol Deposited 2012-07-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa） Fragment：ATPASE, RESIDUES 108-349	Mutation：YES	PO4 PHOSPHATE ION × 1 03V naphthalen-2-ol × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.2；8% PEG-1000, 100 MM NAK PHOSPHATE, PH 6.2	Resolution 1.50 Å R-free 0.228
4B33 Humanised monomeric RadA in complex with napht-2-ol Deposited 2012-07-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa） Fragment：ATPASE, RESIDUES 108-349	Mutation：YES	PO4 PHOSPHATE ION × 1 1NP 1-NAPHTHOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.2；8% PEG-1000, 100 MM NAK PHOSPHATE, PH 6.2	Resolution 1.50 Å R-free 0.227
4B34 Humanised monomeric RadA in complex with 2-amino benzothiazole Deposited 2012-07-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa） Fragment：ATPASE, RESIDUES 108-349	Mutation：YES	PO4 PHOSPHATE ION × 1 ABV 1,3-benzothiazol-2-amine × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.2；8% PEG-1000, 50 MM NAKPHOSPHATE, PH 6.2	Resolution 1.55 Å R-free 0.224
4B35 Humanised monomeric RadA in complex with 4-methylester indole Deposited 2012-07-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa） Fragment：ATPASE, RESIDUES 108-349	Mutation：YES	PO4 PHOSPHATE ION × 1 4ME methyl 1H-indole-4-carboxylate × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.2；8% PEG-1000, 100 MM NAK PHOSPHATE, PH 6.2	Resolution 1.40 Å R-free 0.223
4B3B Humanised monomeric RadA in complex with FHTA tetrapeptide Deposited 2012-07-23	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 A 108–287（180 aa） Fragment：ATPASE, RESIDUES 108-287,300-349 Chain A 300–349（50 aa） Fragment：ATPASE, RESIDUES 108-287,300-349	Mutation：YES Mutation：YES	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.2；pH 6.2	Resolution 1.19 Å R-free 0.167
4B3C Humanised monomeric RadA in complex with 5-hydroxy indole Deposited 2012-07-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–287（180 aa） Fragment：ATPASE, RESIDUES 108-287,300-349 Chain A 300–349（50 aa） Fragment：ATPASE, RESIDUES 108-287,300-349	Mutation：YES Mutation：YES	PO4 PHOSPHATE ION × 1 5H1 1H-indol-5-ol × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.2；8% PEG1000, 100MM NA/K PHOSPHATE PH 6.2	Resolution 1.90 Å R-free 0.261
4B3D Humanised monomeric RadA in complex with 5-methyl indole Deposited 2012-07-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–287（180 aa） Fragment：ATPASE Chain A 300–349（50 aa） Fragment：ATPASE	Mutation：YES Mutation：YES	PO4 PHOSPHATE ION × 1 5MI 5-METHYL INDOLE × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.2；8% PEG-1000, 100 MM NAK PHOSPHATE, PH 6.2	Resolution 1.59 Å R-free 0.212
4B3D Humanised monomeric RadA in complex with 5-methyl indole Deposited 2012-07-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 108–287（180 aa） Fragment：ATPASE Chain C 300–349（50 aa） Fragment：ATPASE	Mutation：YES Mutation：YES	PO4 PHOSPHATE ION × 1 5MI 5-METHYL INDOLE × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.2；8% PEG-1000, 100 MM NAK PHOSPHATE, PH 6.2	Resolution 1.59 Å R-free 0.212
4D6P RADA C-TERMINAL ATPASE DOMAIN FROM PYROCOCCUS FURIOSUS BOUND TO AMPPNP Deposited 2014-11-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa） Fragment：C-TERMINAL ATPASE DOMAIN, UNP RESIDUES 108-349	Mutation：YES	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 GOL GLYCEROL × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.8；60 MM NA2HPO4 PH 6.0, 15% PEG 1000	Resolution 1.48 Å R-free 0.239
4D6P RADA C-TERMINAL ATPASE DOMAIN FROM PYROCOCCUS FURIOSUS BOUND TO AMPPNP Deposited 2014-11-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 108–349（242 aa） Fragment：C-TERMINAL ATPASE DOMAIN, UNP RESIDUES 108-349	Mutation：YES	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 GOL GLYCEROL × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.8；60 MM NA2HPO4 PH 6.0, 15% PEG 1000	Resolution 1.48 Å R-free 0.239
4UQO RADA C-TERMINAL ATPASE DOMAIN FROM PYROCOCCUS FURIOSUS BOUND TO ADP Deposited 2014-06-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa） Fragment：C-TERMINAL ATPASE DOMAIN, RESIDUES 108-349	Mutation：YES	ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.8；60 MM NAPHOSPHATE PH 5.8, 15% PEG1000	Resolution 1.88 Å R-free 0.231
4UQO RADA C-TERMINAL ATPASE DOMAIN FROM PYROCOCCUS FURIOSUS BOUND TO ADP Deposited 2014-06-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 108–349（242 aa） Fragment：C-TERMINAL ATPASE DOMAIN, RESIDUES 108-349	Mutation：YES	ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 NA SODIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.8；60 MM NAPHOSPHATE PH 5.8, 15% PEG1000	Resolution 1.88 Å R-free 0.231
5FOS HUMANISED MONOMERIC RADA IN COMPLEX WITH OLIGOMERISATION PEPTIDE Deposited 2015-11-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 108–349（242 aa） Fragment：ATPASE, UNP RESIDUES 108-349 Chain C 93–108（16 aa） Fragment：OLIGOMERISATION PEPTIDE, UNP RESIDUES 93-108	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	PO4 PHOSPHATE ION × 1 GOL GLYCEROL × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.2；8% PEG-1000, 100 MM NAK PHOSPHATE, PH 6.2	Resolution 1.35 Å R-free 0.181
5FOT HUMANISED MONOMERIC RADA IN COMPLEX WITH FHTU TETRAPEPTIDE Deposited 2015-11-26	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 A 108–349（242 aa） Fragment：ATPASE, UNP RESIDUES 108-349	Mutation：YES	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.2；8% PEG-1000, 100 MM NAK PHOSPHATE, PH 6.2	Resolution 1.19 Å R-free 0.157
5FOU HUMANISED MONOMERIC RADA IN COMPLEX WITH FHPA TETRAPEPTIDE Deposited 2015-11-26	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 A 108–349（242 aa） Fragment：ATPASE, UNP RESIDUES 108-349	Mutation：YES	PO4 PHOSPHATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.2；8% PEG-1000, 100 MM NAK PHOSPHATE, PH 6.2	Resolution 1.50 Å R-free 0.192
5FOV HUMANISED MONOMERIC RADA IN COMPLEX WITH FHTG TETRAPEPTIDE Deposited 2015-11-26	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 A 108–349（242 aa） Fragment：ATPASE, UNP RESIDUES 108-349	Mutation：YES	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.2；8% PEG-1000, 100 MM NAK PHOSPHATE, PH 6.2	Resolution 1.74 Å R-free 0.216
5FOV HUMANISED MONOMERIC RADA IN COMPLEX WITH FHTG TETRAPEPTIDE Deposited 2015-11-26	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 C 108–349（242 aa） Fragment：ATPASE, UNP RESIDUES 108-349	Mutation：YES	PO4 PHOSPHATE ION × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.2；8% PEG-1000, 100 MM NAK PHOSPHATE, PH 6.2	Resolution 1.74 Å R-free 0.216
5FOW HUMANISED MONOMERIC RADA IN COMPLEX WITH WHTA TETRAPEPTIDE Deposited 2015-11-26	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 A 108–349（242 aa） Fragment：ATPASE, UNP RESIDUES 108-349	Mutation：YES	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.2；8% PEG-1000, 100 MM NAK PHOSPHATE, PH 6.2	Resolution 1.80 Å R-free 0.218
5FOW HUMANISED MONOMERIC RADA IN COMPLEX WITH WHTA TETRAPEPTIDE Deposited 2015-11-26	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 C 108–349（242 aa） Fragment：ATPASE, UNP RESIDUES 108-349	Mutation：YES	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.2；8% PEG-1000, 100 MM NAK PHOSPHATE, PH 6.2	Resolution 1.80 Å R-free 0.218
5FOX HUMANISED MONOMERIC RADA IN COMPLEX WITH FHAA TETRAPEPTIDE Deposited 2015-11-26	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 A 108–349（242 aa） Fragment：ATPASE, UNP RESIDUES 108-349	Mutation：YES	PO4 PHOSPHATE ION × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；8% PEG-1000, 100 MM NAK PHOSPHATE, PH 6.2	Resolution 1.30 Å R-free 0.182
5FPK MONOMERIC RADA IN COMPLEX WITH FATA TETRAPEPTIDE Deposited 2015-12-01	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 A 108–349（242 aa） Fragment：ATPASE, UNP RESIDUES 108-349	Mutation：YES	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.2；8% PEG-1000, 100 MM NAK PHOSPHATE, PH 6.2	Resolution 1.34 Å R-free 0.164
5J4H Structure of humanised RadA-mutant humRadA22F in complex with indole-6-carboxylic acid Deposited 2016-04-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa）	Mutation：V168A, I169M, W170Y, I182L, K198D, H199N, I200V, Y201A, V202Y, K221M	1F1 1H-indole-6-carboxylic acid × 1 NA SODIUM ION × 2 CA CALCIUM ION × 1 DMS DIMETHYL SULFOXIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；292 K；0.08M NaCacodylate pH=6.5, 0.16M CaAcetate, 18% PEG 8000, 20% glycerol soaking: 10% DMSO, 5mM compound	Resolution 1.37 Å R-free 0.170
5J4K Structure of humanised RadA-mutant humRadA22F in complex with 1-Indane-6-carboxylic acid Deposited 2016-04-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa）	Mutation：V168A, I169M, W170Y, I182L, K198D, H199N, I200V, Y201A, V202Y, K221M	NA SODIUM ION × 2 CA CALCIUM ION × 1 6FZ 2,3-dihydro-1H-indene-2-carboxylic acid × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；292 K；0.08M NaCacodylate pH=6.5, 0.16M CaAcetate, 18% PEG8000, 20%glycerol soaking: 10% DMSO, 5mM compound	Resolution 1.35 Å R-free 0.164
5J4L Apo-structure of humanised RadA-mutant humRadA22F Deposited 2016-04-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa）	Mutation：V168A, I169M, W170Y, I182L, K198D, H199N, I200V, Y201A, V202Y, K221M	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；292 K；0.08M NaCacodylate, pH=6.5, 0.16M CaAcetate, 18% PEG8000, 20% glycerol	Resolution 1.13 Å R-free 0.145
5JEC Apo-structure of humanised RadA-mutant humRadA33F Deposited 2016-04-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa）	Mutation：;S167K, V168A, I169M, W170Y, N175G, I182L, R183L, D192S, P193G D194S, E195D, K198D, H199N, I200V, Y201A, V202Y, E219S, K221M, I222M, K223V, V232Y ;	CL CHLORIDE ION × 2 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；298 K；22% PEG3350, 0.1M BisTris pH=5.0, 0.2M Li2SO4	Resolution 2.34 Å R-free 0.239
5JEC Apo-structure of humanised RadA-mutant humRadA33F Deposited 2016-04-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 108–349（242 aa）	Mutation：;S167K, V168A, I169M, W170Y, N175G, I182L, R183L, D192S, P193G D194S, E195D, K198D, H199N, I200V, Y201A, V202Y, E219S, K221M, I222M, K223V, V232Y ;	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；298 K；22% PEG3350, 0.1M BisTris pH=5.0, 0.2M Li2SO4	Resolution 2.34 Å R-free 0.239
5JED Apo-structure of humanised RadA-mutant humRadA28 Deposited 2016-04-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa）	Mutation：;S167K, V168A, I169M, W170Y, I182L, K198D, H199N, I200V, Y201A, V202Y, L213Q, V215L, Q216Y, E219S, K221M, I222M, K223V, L225S, V232Y, K263R, H264F, A266R, D267M, L274E, Y275F ;	SO4 SULFATE ION × 1 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；292 K；0.1M NaCacodylate pH=6.5, 5% PEG8000, 40% MPD	Resolution 1.33 Å R-free 0.171
5JEE Apo-structure of humanised RadA-mutant humRadA26F Deposited 2016-04-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa）	Mutation：S167K, V168A, I169M, W170Y, I182L, R183L, K198D, H199N, I200V, Y201A, V202Y, E219S, K221M, I222M	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；292 K；0.1M NaAcetate pH=4.6, 15% PEG20K	Resolution 1.49 Å R-free 0.218
5JFG Structure of humanised RadA-mutant humRadA22F in complex with peptide FHTA Deposited 2016-04-19	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 A 108–349（242 aa） Fragment：UNP residues 108-349	Mutation：YES	DMS DIMETHYL SULFOXIDE × 3 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；292 K；0.08M NaCacodylate pH=6.5, 0.16M CaAcetate, 18% PEG8000, 20% glycerol soaking: 5mM FHTA, 10% DMSO	Resolution 1.77 Å R-free 0.192
5KDD Apo-structure of humanised RadA-mutant humRadA22 Deposited 2016-06-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa）	Mutation：;V168A, I169M, W170Y, I182L, K198D, H199N, I200V, Y201A, V202Y, L213Q, V215L, Q216Y, E219S, D220A, K221M, I222M, K223V, L225S, V232Y, K263R, H264F, A266R, D267M, L274E, Y275F ;	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；297 K；20% PEG3350, 0.2M MgSO4	Resolution 1.99 Å R-free 0.250
5KDD Apo-structure of humanised RadA-mutant humRadA22 Deposited 2016-06-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 108–349（242 aa）	Mutation：;V168A, I169M, W170Y, I182L, K198D, H199N, I200V, Y201A, V202Y, L213Q, V215L, Q216Y, E219S, D220A, K221M, I222M, K223V, L225S, V232Y, K263R, H264F, A266R, D267M, L274E, Y275F ;	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；297 K；20% PEG3350, 0.2M MgSO4	Resolution 1.99 Å R-free 0.250
5L8V Apo-structure of humanised RadA-mutant humRadA4 Deposited 2016-06-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa）	Not recorded	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；292 K；12% PEG20K, 0.1 M MES pH 6.5	Resolution 1.50 Å R-free 0.193
5LB2 Apo-structure of humanised RadA-mutant humRadA2 Deposited 2016-06-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；292 K；25% PEG6000, 100 mM MES pH 7.0	Resolution 2.10 Å R-free 0.252
5LB4 Apo-structure of humanised RadA-mutant humRadA14 Deposited 2016-06-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa）	Mutation：;V168A, I169M, W170Y, Y201A, V202Y, L213Q, V215L, Q216Y, E219S, D220A, K221M, I222M, K223V, L225S, V232Y, H264F, D267M, L274E, Y275F ;	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；292 K；25% PEG4000, 0.1 M Tris pH 8.5	Resolution 1.98 Å R-free 0.260
5LBI Apo-structure of humanised RadA-mutant humRadA3 Deposited 2016-06-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa）	Not recorded	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；292 K；4-8% PEG1000, 100 mM Na/KPO4, pH 5.6	Resolution 1.43 Å R-free 0.193
6TUU Leishmania infantum Rad51 surrogate LiRadA10 in complex with 5,6,7,8-tetrahydro-2-naphthoic acid Deposited 2020-01-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa）	Not recorded	PO4 PHOSPHATE ION × 1 NY5 5,6,7,8-tetrahydronaphthalene-2-carboxylic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；292 K；20 %w/v PEG 1K (Precipitant), 0.1 M Na K Phos 6.2 pH (Buffer), 0.2 M NaCl (Salt)	Resolution 1.74 Å R-free 0.230
6TUU Leishmania infantum Rad51 surrogate LiRadA10 in complex with 5,6,7,8-tetrahydro-2-naphthoic acid Deposited 2020-01-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 108–349（242 aa）	Not recorded	PO4 PHOSPHATE ION × 1 NY5 5,6,7,8-tetrahydronaphthalene-2-carboxylic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；292 K；20 %w/v PEG 1K (Precipitant), 0.1 M Na K Phos 6.2 pH (Buffer), 0.2 M NaCl (Salt)	Resolution 1.74 Å R-free 0.230
6TUU Leishmania infantum Rad51 surrogate LiRadA10 in complex with 5,6,7,8-tetrahydro-2-naphthoic acid Deposited 2020-01-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 108–349（242 aa）	Not recorded	NY5 5,6,7,8-tetrahydronaphthalene-2-carboxylic acid × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；292 K；20 %w/v PEG 1K (Precipitant), 0.1 M Na K Phos 6.2 pH (Buffer), 0.2 M NaCl (Salt)	Resolution 1.74 Å R-free 0.230
6TUU Leishmania infantum Rad51 surrogate LiRadA10 in complex with 5,6,7,8-tetrahydro-2-naphthoic acid Deposited 2020-01-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 108–349（242 aa）	Not recorded	NY5 5,6,7,8-tetrahydronaphthalene-2-carboxylic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；292 K；20 %w/v PEG 1K (Precipitant), 0.1 M Na K Phos 6.2 pH (Buffer), 0.2 M NaCl (Salt)	Resolution 1.74 Å R-free 0.230
6TV3 HumRadA1 in complex with 3-amino-2-naphthoic acid Deposited 2020-01-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa）	Not recorded	NYE 3-azanylnaphthalene-2-carboxylic acid × 1 PO4 PHOSPHATE ION × 1 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；293 K；8% PEG-1000, 100 MM NA/K PHOSPHATE	Resolution 1.50 Å R-free 0.217
6TW3 HumRadA2 in complex with Naphthyl-HPA fragment-peptide chimera Deposited 2020-01-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa）	Not recorded	PO4 PHOSPHATE ION × 2 O0E (2~{S})-1-[(2~{S})-2-[(3-azanylnaphthalen-2-yl)carbonylamino]-3-(1~{H}-imidazol-4-yl)propanoyl]-~{N}-[(2~{S})-1-azanyl-1-oxidanylidene-propan-2-yl]pyrrolidine-2-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；100 mM Na/K phosphate, 6 % PEG1000	Resolution 1.35 Å R-free 0.210
6TW4 HumRadA22F in complex with compound 6 Deposited 2020-01-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa） Fragment：humRadA22F	Mutation：;S167K, V168A, I169M, W170Y, N175G, I182L, R183L, D192S, P193G D194S, E195D, K198D, H199N, I200V, Y201A, V202Y, L213Q, V215L, Q216Y, E219S, D220A, K221M, I222M, K223V, L225S, V232Y, K263R, H264F, A266R, D267M, L274E, Y275F ;	NZW ~{N}-[2-[(2~{S})-2-[[(1~{S})-1-(4-methoxyphenyl)ethyl]carbamoyl]pyrrolidin-1-yl]-2-oxidanylidene-ethyl]quinoline-2-carboxamide × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；298 K；20% PEG8000, 0.08 M Na Cacodylate pH 6.5, 0.16M Ca acetate, 18% glycerol	Resolution 1.73 Å R-free 0.210
6TW9 HumRadA22F in complex with CAM833 Deposited 2020-01-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa） Fragment：humRadA22F	Mutation：;S167K, V168A, I169M, W170Y, N175G, I182L, R183L, D192S, P193G D194S, E195D, K198D, H199N, I200V, Y201A, V202Y, L213Q, V215L, Q216Y, E219S, D220A, K221M, I222M, K223V, L225S, V232Y, K263R, H264F, A266R, D267M, L274E, Y275F ;	O08 ~{N}-[2-[(2~{S},4~{R})-2-[[(1~{S})-1-(2-chloranyl-4-methoxy-phenyl)ethyl]carbamoyl]-4-oxidanyl-pyrrolidin-1-yl]-2-oxidanylidene-ethyl]-6-fluoranyl-quinoline-2-carboxamide × 1 CA CALCIUM ION × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；298 K；20% PEG8000, 0.08 M Na Cacodylate pH 6.5, 0.16M Ca acetate, 18% glycerol	Resolution 1.52 Å R-free 0.172
6XTW HumRadA33F in complex with peptidic inhibitor 6 Deposited 2020-01-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa） Fragment：humRadA22F	Mutation：;S167K, V168A, I169M, W170Y, N175G, I182L, R183L, D192S, P193G D194S, E195D, K198D, H199N, I200V, Y201A, V202Y, L213Q, V215L, Q216Y, E219S, D220A, K221M, I222M, K223V, L225S, V232Y, K263R, H264F, A266R, D267M, L274E, Y275F ;	NZW ~{N}-[2-[(2~{S})-2-[[(1~{S})-1-(4-methoxyphenyl)ethyl]carbamoyl]pyrrolidin-1-yl]-2-oxidanylidene-ethyl]quinoline-2-carboxamide × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；298 K；22% PEG3350, 0.1 M BisTris pH5.0, 0.2 M LiSO4	Resolution 2.31 Å R-free 0.229
6XTW HumRadA33F in complex with peptidic inhibitor 6 Deposited 2020-01-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 108–349（242 aa） Fragment：humRadA22F	Mutation：;S167K, V168A, I169M, W170Y, N175G, I182L, R183L, D192S, P193G D194S, E195D, K198D, H199N, I200V, Y201A, V202Y, L213Q, V215L, Q216Y, E219S, D220A, K221M, I222M, K223V, L225S, V232Y, K263R, H264F, A266R, D267M, L274E, Y275F ;	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；298 K；22% PEG3350, 0.1 M BisTris pH5.0, 0.2 M LiSO4	Resolution 2.31 Å R-free 0.229
6XUF HumRadA1 in complex with 5-Ethyl-N-(1H-indol-5-ylmethyl)-1,3,4-thiadiazol-2-amine in P21 Deposited 2020-01-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa）	Not recorded	PO4 PHOSPHATE ION × 1 O1E 5-Ethyl-N-(1H-indol-5-ylmethyl)-1,3,4-thiadiazol-2-amine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；293 K；50 mM Na/K PHOSPHATE, 5% PEG1000	Resolution 1.24 Å R-free 0.186
6XUJ HumRadA1 in complex with 5-Ethyl-N-(1H-indol-5-ylmethyl)-1,3,4-thiadiazol-2-amine in P21212 Deposited 2020-01-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–349（242 aa）	Not recorded	PO4 PHOSPHATE ION × 1 O1E 5-Ethyl-N-(1H-indol-5-ylmethyl)-1,3,4-thiadiazol-2-amine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；293 K；50 mM Na/K Phosphate, 5% PEG1000	Resolution 1.54 Å R-free 0.205
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 A 107–349（243 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 A 107–349（243 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 B 107–349（243 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 A 107–349（243 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

44 other PDB entries and 57 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	RADA_PYRFU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–349； UniProt 1–349 Author chain B； PDBConstruct 1–349； UniProt 1–349 Author chain C； PDBConstruct 1–349； UniProt 1–349 Author chain D； PDBConstruct 1–349； UniProt 1–349 Author chain E； PDBConstruct 1–349； UniProt 1–349 Author chain F； PDBConstruct 1–349； UniProt 1–349 Author chain G； PDBConstruct 1–349； UniProt 1–349

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	1pzn
Deposition date deposition_date	2003-07-12
Structure title title	Rad51 (RadA)
Keywords keywords	;HEPTAMERIC RING; HEPTAMER; RING; OLIGOMER; RAD51 POLYMERIZATION MOTIF; HELIX-HAIRPIN-HELIX; DNA REPAIR; DNA RECOMBINATION; ATPASE; HOMOLOGOUS RECOMBINATION, RECOMBINATION ;; 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	42.59 Å
Radius of gyration Rg (electron density) rg_electron	41.98 Å
Forward intensity I(0) i0	570769000.00
Molecular weight molecular_weight	196260.0 kDa
Excluded volume excluded_volume	245400 Å³
Envelope volume envelope_volume	317360 Å³
Hydration-shell volume shell_volume	60106 Å³
Envelope diameter envelope_diameter	123.1 Å
Shell Rg shell_rg	50.70 Å
Envelope Rg envelope_rg	40.90 Å
Shape Rg shape_rg	41.95 Å
Total Rg total_rg	42.45 Å
Total atoms total_atoms	13753
Residues n_residues	1712
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	127.4 Å
Rg (real space) rg_real	42.43 Å
Rg uncertainty (real space) rg_real_error	1.06 Å
I(0) (real space) i0_real	5.7080e+08
I(0) uncertainty (real space) i0_real_error	1.1250e+07
Rg (reciprocal space) rg_reciprocal	42.58 Å
I(0) (reciprocal space) i0_reciprocal	570900000.0000
Solution quality estimate total_estimate	0.8923
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	55.1 Å
Skewness Skewness skewness	0.061
Kurtosis Kurtosis kurtosis	-0.822
Angular range angular_range	— – 0.1850 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	73990000.0000
Real-space data points n_real_points	38
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.979; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.659

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	DNA repair and recombination protein rad51
Molecular weight formula_weight	38643.5 kDa
Source method src_method	man
Copy count entity_count	7

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G
Atom count atom_count	13820

MAGEEVKEIDEFEELGFEPATEETPKKKKKEKIIRSIEDLPGVGPATAEKLREAGYDTLEAIAVASPIELKEVAGISEGTALKIIQAARKAANLGTFMRADEYLKKRATIGRISTGSKSLDKLLGGGIETQAITEVFGEFGSGKTQLAHTLAVMVQLPPEEGGLNGSVIWIDTENTFRPERIREIAQNRGLDPDEVLKHIYVARAFNSNHQMLLVQQAEDKIKELLNTDRPVKLLIVDSLTSHFRSEYIGRGALAERQQKLAKHLADLHRLANLYDIAVFVTNQVQARPDAFFGDPTRPIGGHILAHSATLRVYLRKGKGGKRIARLIDAPHLPEGEAVFSITEKGIED

来源 Source

来源生物 organism	Pyrococcus furiosus
NCBI Class编号 ncbi_taxonomy_id	2261
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	7

Entity 3 Entity 3 non-polymer

Description description	IMIDAZOLE
Molecular weight formula_weight	69.1 kDa
Source method src_method	syn
Copy count entity_count	9

Entity 4 Entity 4 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	9

Entity 5 Entity 5 non-polymer

Description description	(4S)-2-METHYL-2,4-PENTANEDIOL
Molecular weight formula_weight	118.2 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	67

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7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d1pzna1
Class class	a — All alpha proteins
Fold Fold fold	a.60 — SAM domain-like
Superfamily Superfamily superfamily	a.60.4 — Rad51 N-terminal domain-like
Family Family family	a.60.4.1 — DNA repair protein Rad51, N-terminal domain

Domain ID domain_id	d1pzna2
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	d1pznb1
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	d1pznc1
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	d1pznd1
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	d1pzne1
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	d1pznf1
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	d1pzng1
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)

CATH v4.4 (8 domains)

Domain ID domain_id	1pznA01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily	20 — 5' to 3' exonuclease, C-terminal subdomain

Domain ID domain_id	1pznA02
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

Domain ID domain_id	1pznB00
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

Domain ID domain_id	1pznC00
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

Domain ID domain_id	1pznD00
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

Domain ID domain_id	1pznE00
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

Domain ID domain_id	1pznF00
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

Domain ID domain_id	1pznG00
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	144.163 Å
Unit-cell length b length_b	193.124 Å
Unit-cell length c length_c	176.930 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	56

Space group space_group	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	—

Resolution resolution	2.850 Å
Low-resolution limit resolution_low	39.120 Å
R factor r_factor	—
R_work r_work	0.2570
R_free r_free	0.3070

fit	/app/data/saxs_computation/pz/1pzn/1pzn.fit
pddf	/app/data/pr_computation/pz/1pzn/1pzn.pr.out
profile	/app/data/saxs_computation/pz/1pzn/1pzn.dat