4ofb

Crystal structure of human BRCA1 BRCT in complex with nonphosphopeptide inhibitor

Method: X-RAY DIFFRACTION D_max: 73.8 Å Quality: GOOD

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

Breast cancer type 1 susceptibility protein

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1646–1859	Fragment：BRCT 1 domain (UNP residues 1646-1859)	nonphosphopeptide inhibitor × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6.5；298 K；0.1M Sodium Cacodylate, 0.1M Magnesium Acetate,24% PEG6000, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.05 Å R-free 0.237

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 4OFB	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1JM7 Solution structure of the BRCA1/BARD1 RING-domain heterodimer Deposited 2001-07-17	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–110（110 aa） Fragment：RING-Domain	Not recorded	ZN ZINC ION × 4	SOLUTION NMR NMR measurement conditions pH 6.8；315 K；Ionic strength (raw mmCIF value) 0.2M NaCl；Pressure ambient NMR measurement conditions pH 6.8；315 K；Ionic strength (raw mmCIF value) 0.2M NaCl；Pressure ambient NMR measurement conditions pH 6.8；315 K；Ionic strength (raw mmCIF value) 0.2M NaCl；Pressure ambient NMR measurement conditions pH 6.8；315 K；Ionic strength (raw mmCIF value) 0.2M NaCl；Pressure ambient NMR sample composition sample 1: 0.8-1.1mM U-15N,13C BRCA1; unlabeled BARD1, 25mM sodium phosphate, 0.2M NaCl, 2mM DTT. Sample 2: 0.8-1.1mM U-15N,13C BARD1; unlabeled BRCA1, 25mM sodium phosphate, 0.2M NaCl, 2mM DTT. Sample 3: 0.8-1.1mM U-15N,13C,85%-2H BRCA1; unlabeled BARD1, 25mM sodium phosphate, 0.2M NaCl, 2mM DTT. SAMPLE 4: 0.8-1.1mM U-15N,13C,85%-2H BARD1; unlabeled BRCA,1 25mM sodium phosphate, 0.2M NaCl, 2mM DTT. \| 90% H2O/10% D2O NMR sample composition 0.8-1.1mM U-15N,13C BARD1; unlabeled BRCA1 25mM sodium phosphate 0.2M NaCl 2mM DTT \| 90% H2O/10% D2O NMR sample composition 0.8-1.1mM U-15N,13C,85%-2H BRCA1; unlabeled BARD1 25mM sodium phosphate 0.2M NaCl 2mM DTT \| 90% H2O/10% D2O NMR sample composition 0.8-1.1mM U-15N,13C,85%-2H BARD1; unlabeled BRCA1 25mM sodium phosphate 0.2M NaCl 2mM DTT \| 90% H2O/10% D2O	Resolution not provided
1JNX Crystal structure of the BRCT repeat region from the breast cancer associated protein, BRCA1 Deposited 2001-07-26	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain X 1646–1859（214 aa） Fragment：residues 1646-1859	Not recorded	NI NICKEL (II) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；298 K；Lithium sulphate, Nickel sulphate, calcium chloride, Tris, pH 8.5,VAPOR DIFFUSION, HANGING DROP at 298K	Resolution 2.50 Å R-free 0.302
1N5O Structural consequences of a cancer-causing BRCA1-BRCT missense mutation Deposited 2002-11-06	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 X 1646–1859（214 aa） Fragment：BRCT (residues 1646-1859)	Mutation：M1775R	CO COBALT (II) ION × 1 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.7；293 K；ammonium sulphate, cobalt chloride, MES, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.80 Å R-free 0.298
1OQA Solution structure of the BRCT-c domain from human BRCA1 Deposited 2003-03-07	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1755–1863（109 aa） Fragment：BRCT-c	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.8；295.9 K；Pressure 1 NMR sample composition 0.7mM BRCT-c; U-15N,13C, 20mM Potassium phosphate buffer pH 6.8, 5 mM KCl, 10 mM d10-DTT, 99.98% D2O \| 99.98% D2O NMR sample composition 1.3 mM BRCT-c; U-15N, 20 mM Potassium phosphate buffer pH 6.8, 5 mM KCl, 10 mM d10-DTT, 93% H2O, 7% D2O \| 93% H2O/7% D2O NMR sample composition 1.3 mM BRCT-c; U-15N, 20 mM Potassium phosphate buffer pH 6.8, 5 mM KCl, 10 mM d10-DTT, 99.98% D2O \| 99.98% D2O	Resolution not provided
1T15 Crystal Structure of the Brca1 BRCT Domains in Complex with the Phosphorylated Interacting Region from Bach1 Helicase Deposited 2004-04-15	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1649–1859（211 aa） Fragment：BCRT 1, BCRT 2	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions MICROBATCH；pH 6.5；291 K；PEG 8000, Ammonium Sulphate, MES, pH 6.5, Microbatch, temperature 291K	Resolution 1.85 Å R-free 0.222
1T29 Crystal structure of the BRCA1 BRCT repeats bound to a phosphorylated BACH1 peptide Deposited 2004-04-20	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1646–1859（214 aa） Fragment：BRCT repeats of BRCA1 (residues 1646-1859)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；295 K；PEG4000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.30 Å R-free 0.266
1T2U Structural basis of phosphopeptide recognition by the BRCT domain of BRCA1: structure of BRCA1 missense variant V1809F Deposited 2004-04-22	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 1646–1859（214 aa） Fragment：BRCT DOMAIN 1646-1859	Mutation：V1809F	CO COBALT (II) ION × 1 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.7；298 K；Ammounium sulphate, cobaltous chloride, MES, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 6.70	Resolution 2.80 Å R-free 0.294
1T2V Structural basis of phospho-peptide recognition by the BRCT domain of BRCA1, structure with phosphopeptide Deposited 2004-04-22	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1646–1859（214 aa） Fragment：BRCT DOMAIN 1646-1859	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.6；298 K；PEG 4000 ammonium acetate, tri-sodium citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 5.60	Resolution 3.30 Å R-free 0.301
1T2V Structural basis of phospho-peptide recognition by the BRCT domain of BRCA1, structure with phosphopeptide Deposited 2004-04-22	Different construct Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1646–1859（214 aa） Fragment：BRCT DOMAIN 1646-1859	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.6；298 K；PEG 4000 ammonium acetate, tri-sodium citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 5.60	Resolution 3.30 Å R-free 0.301
1T2V Structural basis of phospho-peptide recognition by the BRCT domain of BRCA1, structure with phosphopeptide Deposited 2004-04-22	Different construct Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1646–1859（214 aa） Fragment：BRCT DOMAIN 1646-1859	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.6；298 K；PEG 4000 ammonium acetate, tri-sodium citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 5.60	Resolution 3.30 Å R-free 0.301
1T2V Structural basis of phospho-peptide recognition by the BRCT domain of BRCA1, structure with phosphopeptide Deposited 2004-04-22	Different construct Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1646–1859（214 aa） Fragment：BRCT DOMAIN 1646-1859	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.6；298 K；PEG 4000 ammonium acetate, tri-sodium citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 5.60	Resolution 3.30 Å R-free 0.301
1T2V Structural basis of phospho-peptide recognition by the BRCT domain of BRCA1, structure with phosphopeptide Deposited 2004-04-22	Different construct Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 1646–1859（214 aa） Fragment：BRCT DOMAIN 1646-1859	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.6；298 K；PEG 4000 ammonium acetate, tri-sodium citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 5.60	Resolution 3.30 Å R-free 0.301
1T2V Structural basis of phospho-peptide recognition by the BRCT domain of BRCA1, structure with phosphopeptide Deposited 2004-04-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 6 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1646–1859（214 aa） Fragment：BRCT DOMAIN 1646-1859 Chain D 1646–1859（214 aa） Fragment：BRCT DOMAIN 1646-1859	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.6；298 K；PEG 4000 ammonium acetate, tri-sodium citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 5.60	Resolution 3.30 Å R-free 0.301
1T2V Structural basis of phospho-peptide recognition by the BRCT domain of BRCA1, structure with phosphopeptide Deposited 2004-04-22	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 7 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain E 1646–1859（214 aa） Fragment：BRCT DOMAIN 1646-1859	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.6；298 K；PEG 4000 ammonium acetate, tri-sodium citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 5.60	Resolution 3.30 Å R-free 0.301
1Y98 Structure of the BRCT repeats of BRCA1 bound to a CtIP phosphopeptide. Deposited 2004-12-14	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1646–1859（214 aa） Fragment：BRCT 1, BRCT 2	Not recorded	CO COBALT (II) ION × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；AMMONIUM SULPHATE, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.50 Å R-free 0.270
1Y98 Structure of the BRCT repeats of BRCA1 bound to a CtIP phosphopeptide. Deposited 2004-12-14	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1646–1859（214 aa） Fragment：BRCT 1, BRCT 2	Not recorded	CO COBALT (II) ION × 2 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；AMMONIUM SULPHATE, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.50 Å R-free 0.270
2ING X-ray Structure of the BRCA1 BRCT mutant M1775K Deposited 2006-10-07	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 X 1649–1859（211 aa） Fragment：BRCT1, BRCT2	Mutation：M1775K	CO COBALT (II) ION × 1 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.7；291 K；1.4M Ammonium sulfate, 20mM Cobalt chloride, 100mM 2-(N-Morpholino) ethanesulfonic acid, pH 6.7, VAPOR DIFFUSION, SITTING DROP, temperature 291K	Resolution 3.60 Å R-free 0.302
2ING X-ray Structure of the BRCA1 BRCT mutant M1775K Deposited 2006-10-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain X 1649–1859（211 aa） Fragment：BRCT1, BRCT2	Mutation：M1775K	CO COBALT (II) ION × 2 SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.7；291 K；1.4M Ammonium sulfate, 20mM Cobalt chloride, 100mM 2-(N-Morpholino) ethanesulfonic acid, pH 6.7, VAPOR DIFFUSION, SITTING DROP, temperature 291K	Resolution 3.60 Å R-free 0.302
3COJ Crystal Structure of the BRCT Domains of Human BRCA1 in Complex with a Phosphorylated Peptide from Human Acetyl-CoA Carboxylase 1 Deposited 2008-03-28	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain X 1646–1859（214 aa） Fragment：BRCT1 and BRCT2 domains	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；294 K；100 mM sodium acetate (pH 4.5), 25-27% (v/v) PEG400, and 200 mM calcium acetate, VAPOR DIFFUSION, SITTING DROP, temperature 294K	Resolution 3.21 Å R-free 0.307
3COJ Crystal Structure of the BRCT Domains of Human BRCA1 in Complex with a Phosphorylated Peptide from Human Acetyl-CoA Carboxylase 1 Deposited 2008-03-28	Different construct Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1646–1859（214 aa） Fragment：BRCT1 and BRCT2 domains	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；294 K；100 mM sodium acetate (pH 4.5), 25-27% (v/v) PEG400, and 200 mM calcium acetate, VAPOR DIFFUSION, SITTING DROP, temperature 294K	Resolution 3.21 Å R-free 0.307
3COJ Crystal Structure of the BRCT Domains of Human BRCA1 in Complex with a Phosphorylated Peptide from Human Acetyl-CoA Carboxylase 1 Deposited 2008-03-28	Different construct Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1646–1859（214 aa） Fragment：BRCT1 and BRCT2 domains	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；294 K；100 mM sodium acetate (pH 4.5), 25-27% (v/v) PEG400, and 200 mM calcium acetate, VAPOR DIFFUSION, SITTING DROP, temperature 294K	Resolution 3.21 Å R-free 0.307
3COJ Crystal Structure of the BRCT Domains of Human BRCA1 in Complex with a Phosphorylated Peptide from Human Acetyl-CoA Carboxylase 1 Deposited 2008-03-28	Different construct Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1646–1859（214 aa） Fragment：BRCT1 and BRCT2 domains	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；294 K；100 mM sodium acetate (pH 4.5), 25-27% (v/v) PEG400, and 200 mM calcium acetate, VAPOR DIFFUSION, SITTING DROP, temperature 294K	Resolution 3.21 Å R-free 0.307
3COJ Crystal Structure of the BRCT Domains of Human BRCA1 in Complex with a Phosphorylated Peptide from Human Acetyl-CoA Carboxylase 1 Deposited 2008-03-28	Different construct Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1646–1859（214 aa） Fragment：BRCT1 and BRCT2 domains	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；294 K；100 mM sodium acetate (pH 4.5), 25-27% (v/v) PEG400, and 200 mM calcium acetate, VAPOR DIFFUSION, SITTING DROP, temperature 294K	Resolution 3.21 Å R-free 0.307
3COJ Crystal Structure of the BRCT Domains of Human BRCA1 in Complex with a Phosphorylated Peptide from Human Acetyl-CoA Carboxylase 1 Deposited 2008-03-28	Different construct Different experimental conditions Different structure-quality metrics	Assembly 6 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 1646–1859（214 aa） Fragment：BRCT1 and BRCT2 domains	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；294 K；100 mM sodium acetate (pH 4.5), 25-27% (v/v) PEG400, and 200 mM calcium acetate, VAPOR DIFFUSION, SITTING DROP, temperature 294K	Resolution 3.21 Å R-free 0.307
3COJ Crystal Structure of the BRCT Domains of Human BRCA1 in Complex with a Phosphorylated Peptide from Human Acetyl-CoA Carboxylase 1 Deposited 2008-03-28	Different construct Different experimental conditions Different structure-quality metrics	Assembly 7 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 1646–1859（214 aa） Fragment：BRCT1 and BRCT2 domains	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；294 K；100 mM sodium acetate (pH 4.5), 25-27% (v/v) PEG400, and 200 mM calcium acetate, VAPOR DIFFUSION, SITTING DROP, temperature 294K	Resolution 3.21 Å R-free 0.307
3COJ Crystal Structure of the BRCT Domains of Human BRCA1 in Complex with a Phosphorylated Peptide from Human Acetyl-CoA Carboxylase 1 Deposited 2008-03-28	Different construct Different experimental conditions Different structure-quality metrics	Assembly 8 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain G 1646–1859（214 aa） Fragment：BRCT1 and BRCT2 domains	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；294 K；100 mM sodium acetate (pH 4.5), 25-27% (v/v) PEG400, and 200 mM calcium acetate, VAPOR DIFFUSION, SITTING DROP, temperature 294K	Resolution 3.21 Å R-free 0.307
3K0H The crystal structure of BRCA1 BRCT in complex with a minimal recognition tetrapeptide with an amidated C-terminus Deposited 2009-09-24	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1646–1859（214 aa） Fragment：BRCT Domain (UNP residues 1646 to 1859)	Not recorded	NI NICKEL (II) ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.3；298 K；Tris-HCl, Li2SO4, NiCl2, pH 7.3, VAPOR DIFFUSION, temperature 298K	Resolution 2.70 Å R-free 0.296
3K0K Crystal Structure of BRCA1 BRCT in complex with a minimal recognition tetrapeptide with a free carboxy C-terminus. Deposited 2009-09-24	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1646–1859（214 aa） Fragment：BRCT Domain (UNP residues 1646 to 1859)	Not recorded	NI NICKEL (II) ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.3；298 K；Li2SO4, Tris-HCl, NiCl2, pH 7.3, VAPOR DIFFUSION, temperature 298K	Resolution 2.70 Å R-free 0.299
3K15 Crystal Structure of BRCA1 BRCT D1840T in complex with a minimal recognition tetrapeptide with an amidated C-terminus Deposited 2009-09-25	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1646–1859（214 aa） Fragment：BRCT Domain (UNP residues 1646 to 1859)	Mutation：D1840T	NI NICKEL (II) ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；298 K；Li2SO4, Tris-HCl, NiCl2, pH 8.5, VAPOR DIFFUSION, temperature 298K	Resolution 2.80 Å R-free 0.280
3K16 Crystal Structure of BRCA1 BRCT D1840T in complex with a minimal recognition tetrapeptide with a free carboxy C-terminus Deposited 2009-09-25	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1646–1859（214 aa） Fragment：BRCT Domain	Mutation：D1840T	NI NICKEL (II) ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；298 K；Li2SO4, Tris-HCl, NiCl2, pH 8.5, VAPOR DIFFUSION, temperature 298K	Resolution 3.00 Å R-free 0.288
3PXA Impact of BRCA1 BRCT domain missense substitutions on phospho-peptide recognition: G1656D Deposited 2010-12-09	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 1646–1859（214 aa） Fragment：BRCT Domain, UNP residues 1646-1859	Mutation：G1656D	NI NICKEL (II) ION × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；1.0M Li2SO4 100mM Tris 5mM CaCl2 10mM NiCl2 , pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.55 Å R-free 0.261
3PXB Impact of BRCA1 BRCT domain missense substitutions on phospho-peptide recognition: T1700A Deposited 2010-12-09	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 1646–1859（214 aa） Fragment：BRCT domain, UNP residues 1646-1859	Mutation：T1700A	SO4 SULFATE ION × 1 NI NICKEL (II) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；0.8 M Li2SO4 100 mM TRIS 5mM CaCl2 10 mM NiCl2, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.274
3PXC Impact of BRCA1 BRCT domain missense substitutions on phospho-peptide recognition: R1699Q Deposited 2010-12-09	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 X 1646–1859（214 aa） Fragment：BRCT domain, UNP residues 1646-1859	Mutation：R1699Q	SO4 SULFATE ION × 1 NI NICKEL (II) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；0.8M Li2SO4 100mM Tris 5mM CaCl2 10mM NiCl2, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.80 Å R-free 0.270
3PXD Impact of BRCA1 BRCT domain missense substitutions on phospho-peptide recognition: R1835P Deposited 2010-12-09	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 1646–1859（214 aa） Fragment：BRCT Domain, UNP residues 1646-1859	Mutation：R1835P	SO4 SULFATE ION × 1 NI NICKEL (II) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；0.8M Li2SO4 100 mM Tris 5mM CaCl2 10mM NiCl2, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.80 Å R-free 0.281
3PXE Impact of BRCA1 BRCT domain missense substitutions on phospho-peptide recognition: E1836K Deposited 2010-12-09	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1646–1859（214 aa） Fragment：BRCT domain, UNP residues 1646-1859	Mutation：E1836K	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；50mM MES 0.15M (NH4)2SO4 26% PEG 8000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.85 Å R-free 0.266
3PXE Impact of BRCA1 BRCT domain missense substitutions on phospho-peptide recognition: E1836K Deposited 2010-12-09	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1646–1859（214 aa） Fragment：BRCT domain, UNP residues 1646-1859	Mutation：E1836K	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；50mM MES 0.15M (NH4)2SO4 26% PEG 8000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.85 Å R-free 0.266
3PXE Impact of BRCA1 BRCT domain missense substitutions on phospho-peptide recognition: E1836K Deposited 2010-12-09	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1646–1859（214 aa） Fragment：BRCT domain, UNP residues 1646-1859	Mutation：E1836K	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；50mM MES 0.15M (NH4)2SO4 26% PEG 8000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.85 Å R-free 0.266
3PXE Impact of BRCA1 BRCT domain missense substitutions on phospho-peptide recognition: E1836K Deposited 2010-12-09	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1646–1859（214 aa） Fragment：BRCT domain, UNP residues 1646-1859	Mutation：E1836K	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；50mM MES 0.15M (NH4)2SO4 26% PEG 8000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.85 Å R-free 0.266
4IFI Structure of human BRCA1 BRCT in complex with BAAT peptide Deposited 2012-12-14	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1646–1859（214 aa） Fragment：BRCT domain, UNP residues 1650-1859	Not recorded	ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.8；293 K；30% PEG 6000, 1M LiCl. 0.1M Sodium Acetate , pH 4.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.20 Å R-free 0.261
4IFI Structure of human BRCA1 BRCT in complex with BAAT peptide Deposited 2012-12-14	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1646–1859（214 aa） Fragment：BRCT domain, UNP residues 1650-1859	Not recorded	ACT ACETATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.8；293 K；30% PEG 6000, 1M LiCl. 0.1M Sodium Acetate , pH 4.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.20 Å R-free 0.261
4IGK Structure of human BRCA1 BRCT in complex with ATRIP peptide Deposited 2012-12-17	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1646–1859（214 aa） Fragment：BRCT domain, UNP residues 1646-1859	Not recorded	GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；20% PEG3350, 0.2 M ammonium acetate, 8% glycerol, 0.1 M HEPES pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.75 Å R-free 0.204
4IGK Structure of human BRCA1 BRCT in complex with ATRIP peptide Deposited 2012-12-17	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1646–1859（214 aa） Fragment：BRCT domain, UNP residues 1646-1859	Not recorded	GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；20% PEG3350, 0.2 M ammonium acetate, 8% glycerol, 0.1 M HEPES pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.75 Å R-free 0.204
4JLU Crystal structure of BRCA1 BRCT with doubly phosphorylated Abraxas Deposited 2013-03-13	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1649–1859（211 aa） Fragment：UNP RESIDUES 1649-1859	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；pH 6.5, VAPOR DIFFUSION, HANGING DROP	Resolution 3.50 Å R-free 0.327
4U4A Complex Structure of BRCA1 BRCT with singly phospho Abraxas Deposited 2014-07-23	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1646–1859（214 aa） Fragment：BRCT (UNP RESIDUES 1646-1859)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；295 K；0.01M Cobalt Chloride, 0.1 M(MES), pH 6.5, 30% PEG Mono Methyl Ether (MME) 5000	Resolution 3.51 Å R-free 0.362
4U4A Complex Structure of BRCA1 BRCT with singly phospho Abraxas Deposited 2014-07-23	Different construct Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1646–1859（214 aa） Fragment：BRCT (UNP RESIDUES 1646-1859)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；295 K；0.01M Cobalt Chloride, 0.1 M(MES), pH 6.5, 30% PEG Mono Methyl Ether (MME) 5000	Resolution 3.51 Å R-free 0.362
4U4A Complex Structure of BRCA1 BRCT with singly phospho Abraxas Deposited 2014-07-23	Different construct Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1646–1859（214 aa） Fragment：BRCT (UNP RESIDUES 1646-1859)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；295 K；0.01M Cobalt Chloride, 0.1 M(MES), pH 6.5, 30% PEG Mono Methyl Ether (MME) 5000	Resolution 3.51 Å R-free 0.362
4Y18 Structure of BRCA1 BRCT domains in complex with Abraxas double phosphorylated peptide Deposited 2015-02-06	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1646–1859（214 aa） Fragment：BRCT domains, UNP residues 1646-1859	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；HEPES, Ammonium Sulphate, PEG 4000.	Resolution 3.50 Å R-free 0.297
4Y18 Structure of BRCA1 BRCT domains in complex with Abraxas double phosphorylated peptide Deposited 2015-02-06	Different construct Different experimental conditions Different structure-quality metrics	Assembly 10 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain G 1646–1859（214 aa） Fragment：BRCT domains, UNP residues 1646-1859	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；HEPES, Ammonium Sulphate, PEG 4000.	Resolution 3.50 Å R-free 0.297
4Y18 Structure of BRCA1 BRCT domains in complex with Abraxas double phosphorylated peptide Deposited 2015-02-06	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 11 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain G 1646–1859（214 aa） Fragment：BRCT domains, UNP residues 1646-1859 Chain H 1646–1859（214 aa） Fragment：BRCT domains, UNP residues 1646-1859	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；HEPES, Ammonium Sulphate, PEG 4000.	Resolution 3.50 Å R-free 0.297
4Y18 Structure of BRCA1 BRCT domains in complex with Abraxas double phosphorylated peptide Deposited 2015-02-06	Different construct Different experimental conditions Different structure-quality metrics	Assembly 12 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 1646–1859（214 aa） Fragment：BRCT domains, UNP residues 1646-1859	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；HEPES, Ammonium Sulphate, PEG 4000.	Resolution 3.50 Å R-free 0.297
4Y18 Structure of BRCA1 BRCT domains in complex with Abraxas double phosphorylated peptide Deposited 2015-02-06	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1646–1859（214 aa） Fragment：BRCT domains, UNP residues 1646-1859 Chain B 1646–1859（214 aa） Fragment：BRCT domains, UNP residues 1646-1859	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；HEPES, Ammonium Sulphate, PEG 4000.	Resolution 3.50 Å R-free 0.297
4Y18 Structure of BRCA1 BRCT domains in complex with Abraxas double phosphorylated peptide Deposited 2015-02-06	Different construct Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1646–1859（214 aa） Fragment：BRCT domains, UNP residues 1646-1859	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；HEPES, Ammonium Sulphate, PEG 4000.	Resolution 3.50 Å R-free 0.297
4Y18 Structure of BRCA1 BRCT domains in complex with Abraxas double phosphorylated peptide Deposited 2015-02-06	Different construct Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1646–1859（214 aa） Fragment：BRCT domains, UNP residues 1646-1859	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；HEPES, Ammonium Sulphate, PEG 4000.	Resolution 3.50 Å R-free 0.297
4Y18 Structure of BRCA1 BRCT domains in complex with Abraxas double phosphorylated peptide Deposited 2015-02-06	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1646–1859（214 aa） Fragment：BRCT domains, UNP residues 1646-1859 Chain E 1646–1859（214 aa） Fragment：BRCT domains, UNP residues 1646-1859	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；HEPES, Ammonium Sulphate, PEG 4000.	Resolution 3.50 Å R-free 0.297
4Y18 Structure of BRCA1 BRCT domains in complex with Abraxas double phosphorylated peptide Deposited 2015-02-06	Different construct Different experimental conditions Different structure-quality metrics	Assembly 6 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1646–1859（214 aa） Fragment：BRCT domains, UNP residues 1646-1859	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；HEPES, Ammonium Sulphate, PEG 4000.	Resolution 3.50 Å R-free 0.297
4Y18 Structure of BRCA1 BRCT domains in complex with Abraxas double phosphorylated peptide Deposited 2015-02-06	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 7 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain D 1646–1859（214 aa） Fragment：BRCT domains, UNP residues 1646-1859 Chain F 1646–1859（214 aa） Fragment：BRCT domains, UNP residues 1646-1859	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；HEPES, Ammonium Sulphate, PEG 4000.	Resolution 3.50 Å R-free 0.297
4Y18 Structure of BRCA1 BRCT domains in complex with Abraxas double phosphorylated peptide Deposited 2015-02-06	Different construct Different experimental conditions Different structure-quality metrics	Assembly 8 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 1646–1859（214 aa） Fragment：BRCT domains, UNP residues 1646-1859	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；HEPES, Ammonium Sulphate, PEG 4000.	Resolution 3.50 Å R-free 0.297
4Y18 Structure of BRCA1 BRCT domains in complex with Abraxas double phosphorylated peptide Deposited 2015-02-06	Different construct Different experimental conditions Different structure-quality metrics	Assembly 9 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 1646–1859（214 aa） Fragment：BRCT domains, UNP residues 1646-1859	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；HEPES, Ammonium Sulphate, PEG 4000.	Resolution 3.50 Å R-free 0.297
4Y2G Structure of BRCA1 BRCT domains in complex with Abraxas single phosphorylated peptide Deposited 2015-02-09	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1646–1859（214 aa） Fragment：UNP residues 1646-1859	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；291 K；Lithium chloride, Tris, PEG 6000	Resolution 2.50 Å R-free 0.252
6G2I Filament of acetyl-CoA carboxylase and BRCT domains of BRCA1 (ACC-BRCT) at 5.9 A resolution Deposited 2018-03-23	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: octadecameric	Chain H 1667–1880（214 aa） Chain K 1667–1880（214 aa） Chain M 1667–1880（214 aa） Chain O 1667–1880（214 aa） Chain S 1667–1880（214 aa） Chain U 1667–1880（214 aa） Chain W 1667–1880（214 aa） Chain Y 1667–1880（214 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 5.90 Å
7LYB Cryo-EM structure of the human nucleosome core particle in complex with BRCA1-BARD1-UbcH5c Deposited 2021-03-06	Different construct 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: tridecameric	Chain M 1–100（100 aa） Fragment：RING domain (UNP residues 1-100)	Not recorded	ZN ZINC ION × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.28 Å
8GRQ Cryo-EM structure of BRCA1/BARD1 bound to H2AK127-UbcH5c-Ub nucleosome Deposited 2022-09-02	Different construct 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: tridecameric	Chain K 6–97（92 aa）	Not recorded	ZN ZINC ION × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.87 Å
8RS8 Crystal structure of BRCA1 BRCTs in complex with a RIF1 phosphopeptide Deposited 2024-01-24	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1646–1859（214 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 9	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；287 K；55.5 mM MES, 44.5 mM Imidazole, 120 mM Diethylene glycol, 120 mM Triethylene-glycol, 120 mM Tetraethylene glycol, 120 mM Pentaethylene glycol, 20% (v/v) Ethylene glycol, 10% (w/v) PEG 8000	Resolution 1.31 Å R-free 0.179
8RS8 Crystal structure of BRCA1 BRCTs in complex with a RIF1 phosphopeptide Deposited 2024-01-24	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1646–1859（214 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 7 IMD IMIDAZOLE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；287 K；55.5 mM MES, 44.5 mM Imidazole, 120 mM Diethylene glycol, 120 mM Triethylene-glycol, 120 mM Tetraethylene glycol, 120 mM Pentaethylene glycol, 20% (v/v) Ethylene glycol, 10% (w/v) PEG 8000	Resolution 1.31 Å R-free 0.179
8RS8 Crystal structure of BRCA1 BRCTs in complex with a RIF1 phosphopeptide Deposited 2024-01-24	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1646–1859（214 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 13 IMD IMIDAZOLE × 1 PEG DI(HYDROXYETHYL)ETHER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；287 K；55.5 mM MES, 44.5 mM Imidazole, 120 mM Diethylene glycol, 120 mM Triethylene-glycol, 120 mM Tetraethylene glycol, 120 mM Pentaethylene glycol, 20% (v/v) Ethylene glycol, 10% (w/v) PEG 8000	Resolution 1.31 Å R-free 0.179
8RS8 Crystal structure of BRCA1 BRCTs in complex with a RIF1 phosphopeptide Deposited 2024-01-24	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1646–1859（214 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；287 K；55.5 mM MES, 44.5 mM Imidazole, 120 mM Diethylene glycol, 120 mM Triethylene-glycol, 120 mM Tetraethylene glycol, 120 mM Pentaethylene glycol, 20% (v/v) Ethylene glycol, 10% (w/v) PEG 8000	Resolution 1.31 Å R-free 0.179
9QPX BRCA1 BRCT tandem repeat with RNA polymerase II pSer5-CTD peptide Deposited 2025-03-30	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1646–1859（214 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；277 K；0.1M PCB buffer (sodium propionate, sodium cacodylate, BIS-TRIS propane in the molar ratios 2:1:2) pH 6, 25%PEG 1500	Resolution 3.00 Å R-free 0.312
9QPX BRCA1 BRCT tandem repeat with RNA polymerase II pSer5-CTD peptide Deposited 2025-03-30	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 1646–1859（214 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；277 K；0.1M PCB buffer (sodium propionate, sodium cacodylate, BIS-TRIS propane in the molar ratios 2:1:2) pH 6, 25%PEG 1500	Resolution 3.00 Å R-free 0.312
9QPX BRCA1 BRCT tandem repeat with RNA polymerase II pSer5-CTD peptide Deposited 2025-03-30	Different construct Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1646–1859（214 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；277 K；0.1M PCB buffer (sodium propionate, sodium cacodylate, BIS-TRIS propane in the molar ratios 2:1:2) pH 6, 25%PEG 1500	Resolution 3.00 Å R-free 0.312
9QPX BRCA1 BRCT tandem repeat with RNA polymerase II pSer5-CTD peptide Deposited 2025-03-30	Different construct Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1646–1859（214 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；277 K；0.1M PCB buffer (sodium propionate, sodium cacodylate, BIS-TRIS propane in the molar ratios 2:1:2) pH 6, 25%PEG 1500	Resolution 3.00 Å R-free 0.312

31 other PDB entries and 70 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	BRCA1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–214； UniProt 1646–1859

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	4ofb
Deposition date deposition_date	2014-01-14
Structure title title	Crystal structure of human BRCA1 BRCT in complex with nonphosphopeptide inhibitor
Keywords keywords	BRCT domain, DSB DNA damage repair, non-phosphorylated peptide, PROTEIN BINDING; PROTEIN BINDING
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	19.60 Å
Radius of gyration Rg (electron density) rg_electron	18.86 Å
Forward intensity I(0) i0	11585800.00
Molecular weight molecular_weight	25497.0 kDa
Excluded volume excluded_volume	31977 Å³
Envelope volume envelope_volume	36924 Å³
Hydration-shell volume shell_volume	17085 Å³
Envelope diameter envelope_diameter	73.2 Å
Shell Rg shell_rg	24.51 Å
Envelope Rg envelope_rg	19.34 Å
Shape Rg shape_rg	18.84 Å
Total Rg total_rg	19.77 Å
Total atoms total_atoms	1791
Residues n_residues	219
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	73.8 Å
Rg (real space) rg_real	19.67 Å
Rg uncertainty (real space) rg_real_error	0.65 Å
I(0) (real space) i0_real	1.1590e+07
I(0) uncertainty (real space) i0_real_error	1.5750e+05
Rg (reciprocal space) rg_reciprocal	19.66 Å
I(0) (reciprocal space) i0_reciprocal	11590000.0000
Solution quality estimate total_estimate	0.7974
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	21.8 Å
Skewness Skewness skewness	0.527
Kurtosis Kurtosis kurtosis	0.057
Angular range angular_range	— – 0.4050 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	3754000.0000
Real-space data points n_real_points	72
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.533; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.765; Smooth: 0.998

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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	Breast cancer type 1 susceptibility protein
Molecular weight formula_weight	24531.2 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	1791

VNKRMSMVVSGLTPEEFMLVYKFARKHHITLTNLITEETTHVVMKTDAEFVCERTLKYFLGIAGGKWVVSYFWVTQSIKERKMLNEHDFEVRGDVVNGRNHQGPKRARESQDRKIFRGLEICCYGPFTNMPTDQLEWMVQLCGASVVKELSSFTLGTGVHPIVVVQPDAWTEDNGFHAIGQMCEAPVVTREWVLDSVALYQCQELDTYLIPQIP

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	nonphosphopeptide inhibitor
Molecular weight formula_weight	1653.8 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

XTIDFDEYRFRKTX

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d4ofba1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.15 — BRCT domain
Superfamily Superfamily superfamily	c.15.1 — BRCT domain
Family Family family	c.15.1.3 — BRCT domain

Domain ID domain_id	d4ofba2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.15 — BRCT domain
Superfamily Superfamily superfamily	c.15.1 — BRCT domain
Family Family family	c.15.1.3 — BRCT domain

CATH v4.4 (2 domains)

Domain ID domain_id	4ofbA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	10190 — BRCT domain

Domain ID domain_id	4ofbA02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	10190 — BRCT domain

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8. Citations (1)

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Unit-cell length a length_a	37.811 Å
Unit-cell length b length_b	37.811 Å
Unit-cell length c length_c	175.993 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 41
Space-group number int_tables_number	76
Crystal system crystal_system	—

Resolution resolution	3.050 Å
Low-resolution limit resolution_low	37.811 Å
R factor r_factor	0.2118
R_work r_work	0.2105
R_free r_free	0.2375

fit	/app/data/saxs_computation/of/4ofb/4ofb.fit
pddf	/app/data/pr_computation/of/4ofb/4ofb.pr.out
profile	/app/data/saxs_computation/of/4ofb/4ofb.dat

Crystal structure of human BRCA1 BRCT in complex with nonphosphopeptide inhibitor

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

Breast cancer type 1 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

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)