SAXSdb — 3kdf

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

Replication protein A 14 kDa subunit

Homo sapiens

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 1–121 Chain C； UniProt 1–121	Mutation：M1S Non-standard monomer：Yes (specific site not provided by mmCIF)	Replication protein A 32 kDa subunit × 2 （P15927） EDO 1,2-ETHANEDIOL × 7	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7；293 K；11% PEG 8000, 50 mM BisTris-propane pH 7.0, 50 mM NaCl, 5 mM HEPES pH 7.0, 0.3 mM TCEP, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 1.98 Å R-free 0.206
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–121	Mutation：M1S Non-standard monomer：Yes (specific site not provided by mmCIF)	Replication protein A 32 kDa subunit × 1 （P15927） EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7；293 K；11% PEG 8000, 50 mM BisTris-propane pH 7.0, 50 mM NaCl, 5 mM HEPES pH 7.0, 0.3 mM TCEP, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 1.98 Å R-free 0.206
3	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 1–121	Mutation：M1S Non-standard monomer：Yes (specific site not provided by mmCIF)	Replication protein A 32 kDa subunit × 1 （P15927） EDO 1,2-ETHANEDIOL × 5	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7；293 K；11% PEG 8000, 50 mM BisTris-propane pH 7.0, 50 mM NaCl, 5 mM HEPES pH 7.0, 0.3 mM TCEP, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 1.98 Å R-free 0.206

Other States of the Same Protein in the Database

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

Other PDB	Difference from Current Entry 3KDF	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1L1O Structure of the human Replication Protein A (RPA) trimerization core Deposited 2002-02-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 1–121（121 aa） Fragment：RPA14 Chain D 1–121（121 aa） Fragment：RPA14	Not recorded	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.8；300 K；0.1 M Hepes, 9% glycerol, and 1.6 M ammonium sulfate, pH 7.8, VAPOR DIFFUSION, SITTING DROP, temperature 300K	Resolution 2.80 Å R-free 0.282
1QUQ COMPLEX OF REPLICATION PROTEIN A SUBUNITS RPA14 AND RPA32 Deposited 1999-07-02	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 1–121（121 aa） Fragment：RPA14 Chain D 1–121（121 aa） Fragment：RPA14	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；0.1 M MES, 0.75 M AMMONIUM SULPHATE, 20% PEG 8K, 10 MM DTT., pH 6.50	Resolution 2.50 Å R-free 0.291
1QUQ COMPLEX OF REPLICATION PROTEIN A SUBUNITS RPA14 AND RPA32 Deposited 1999-07-02	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–121（121 aa） Fragment：RPA14	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；0.1 M MES, 0.75 M AMMONIUM SULPHATE, 20% PEG 8K, 10 MM DTT., pH 6.50	Resolution 2.50 Å R-free 0.291
1QUQ COMPLEX OF REPLICATION PROTEIN A SUBUNITS RPA14 AND RPA32 Deposited 1999-07-02	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–121（121 aa） Fragment：RPA14	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；0.1 M MES, 0.75 M AMMONIUM SULPHATE, 20% PEG 8K, 10 MM DTT., pH 6.50	Resolution 2.50 Å R-free 0.291
2PI2 Full-length Replication protein A subunits RPA14 and RPA32 Deposited 2007-04-12	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 1–121（121 aa）	Not recorded	DIO 1,4-DIETHYLENE DIOXIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；10% dioxane, 0.1 M MES pH 6.5, 39% saturated ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.00 Å R-free 0.255
2PI2 Full-length Replication protein A subunits RPA14 and RPA32 Deposited 2007-04-12	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 1–121（121 aa）	Not recorded	DIO 1,4-DIETHYLENE DIOXIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；10% dioxane, 0.1 M MES pH 6.5, 39% saturated ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.00 Å R-free 0.255
2PI2 Full-length Replication protein A subunits RPA14 and RPA32 Deposited 2007-04-12	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain G 1–121（121 aa）	Not recorded	DIO 1,4-DIETHYLENE DIOXIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；10% dioxane, 0.1 M MES pH 6.5, 39% saturated ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.00 Å R-free 0.255
2PI2 Full-length Replication protein A subunits RPA14 and RPA32 Deposited 2007-04-12	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 1–121（121 aa）	Not recorded	DIO 1,4-DIETHYLENE DIOXIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；10% dioxane, 0.1 M MES pH 6.5, 39% saturated ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.00 Å R-free 0.255
2PQA Crystal Structure of Full-length Human RPA 14/32 Heterodimer Deposited 2007-05-01	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–121（121 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；0.1 M Bicine pH 9, 20% saturated ammonium sulfate, 10% acetonitrile, VAPOR DIFFUSION, HANGING DROP, temperature 293K, pH 9.0	Resolution 2.50 Å R-free 0.280
2PQA Crystal Structure of Full-length Human RPA 14/32 Heterodimer Deposited 2007-05-01	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–121（121 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；0.1 M Bicine pH 9, 20% saturated ammonium sulfate, 10% acetonitrile, VAPOR DIFFUSION, HANGING DROP, temperature 293K, pH 9.0	Resolution 2.50 Å R-free 0.280
2Z6K Crystal structure of full-length human RPA14/32 heterodimer Deposited 2007-08-03	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–121（121 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 5.9；293 K；0.95M KNa tartrate, 0.1M MES, 10mM DTT, pH 5.9, EVAPORATION, temperature 293K	Resolution 3.00 Å R-free 0.269
2Z6K Crystal structure of full-length human RPA14/32 heterodimer Deposited 2007-08-03	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–121（121 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 5.9；293 K；0.95M KNa tartrate, 0.1M MES, 10mM DTT, pH 5.9, EVAPORATION, temperature 293K	Resolution 3.00 Å R-free 0.269
8RK2 Human Replication protein A (RPA; trimeric core) - ssDNA complex Deposited 2023-12-22	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 1–121（121 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
9MJ5 Catalytic domain of human DNA polymerase alpha in complex with DNA and RPA Deposited 2024-12-13	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 4 PDB declaration: hexameric	Chain A 1–121（121 aa）	Not recorded	ZN ZINC ION × 1 MG MAGNESIUM ION × 1 DCP 2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
9PD3 NER dual incision complex - DuIS Deposited 2025-06-30	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 15 PDB declaration: 17-meric	Chain P 1–121（121 aa）	Not recorded	SF4 IRON/SULFUR CLUSTER × 1 ZN ZINC ION × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
9PD4 NER dual incision complex - DuIM Deposited 2025-06-30	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 14 PDB declaration: hexadecameric	Chain P 1–121（121 aa）	Not recorded	SF4 IRON/SULFUR CLUSTER × 1 ZN ZINC ION × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å

9 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	RFA3_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–121； UniProt 1–121 Author chain C； PDBConstruct 1–121； UniProt 1–121

Replication protein A 32 kDa subunit

Homo sapiens

UniProt P15927

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain B； UniProt 41–172 Chain D； UniProt 41–172	Fragment：Residues 41-172 Mutation：A41S Non-standard monomer：Yes (specific site not provided by mmCIF)	Replication protein A 14 kDa subunit × 2 （P35244） EDO 1,2-ETHANEDIOL × 7	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7；293 K；11% PEG 8000, 50 mM BisTris-propane pH 7.0, 50 mM NaCl, 5 mM HEPES pH 7.0, 0.3 mM TCEP, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 1.98 Å R-free 0.206
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 41–172	Fragment：Residues 41-172 Mutation：A41S Non-standard monomer：Yes (specific site not provided by mmCIF)	Replication protein A 14 kDa subunit × 1 （P35244） EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7；293 K；11% PEG 8000, 50 mM BisTris-propane pH 7.0, 50 mM NaCl, 5 mM HEPES pH 7.0, 0.3 mM TCEP, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 1.98 Å R-free 0.206
3	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain D； UniProt 41–172	Fragment：Residues 41-172 Mutation：A41S Non-standard monomer：Yes (specific site not provided by mmCIF)	Replication protein A 14 kDa subunit × 1 （P35244） EDO 1,2-ETHANEDIOL × 5	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7；293 K；11% PEG 8000, 50 mM BisTris-propane pH 7.0, 50 mM NaCl, 5 mM HEPES pH 7.0, 0.3 mM TCEP, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 1.98 Å R-free 0.206

Other States of the Same Protein in the Database

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

Other PDB	Difference from Current Entry 3KDF	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1DPU SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF HUMAN RPA32 COMPLEXED WITH UNG2(73-88) Deposited 1999-12-27	Different construct Different mutation/modification 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 202–270（69 aa） Fragment：C-TERMINAL DOMAIN (RESIDUES 172-270)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 25mM PHOSPHATE, 50mM NACL；Pressure AMBIENT NMR sample composition 1MM RPA32(172-270) U- 15N,13C; 1.2 MM UNG2(73- 88) NA; 25MM PHOSPHATE BUFFER NA; 50MM NACL; 5 MM DTT NA	Resolution not provided
1L1O Structure of the human Replication Protein A (RPA) trimerization core Deposited 2002-02-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 44–171（128 aa） Fragment：RPA32 central domain (residues 44-171) Chain E 44–171（128 aa） Fragment：RPA32 central domain (residues 44-171)	Not recorded	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.8；300 K；0.1 M Hepes, 9% glycerol, and 1.6 M ammonium sulfate, pH 7.8, VAPOR DIFFUSION, SITTING DROP, temperature 300K	Resolution 2.80 Å R-free 0.282
1QUQ COMPLEX OF REPLICATION PROTEIN A SUBUNITS RPA14 AND RPA32 Deposited 1999-07-02	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 43–171（129 aa） Fragment：CENTRAL DOMAIN, RESIDUES 43-171 Chain C 43–171（129 aa） Fragment：CENTRAL DOMAIN, RESIDUES 43-171	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；0.1 M MES, 0.75 M AMMONIUM SULPHATE, 20% PEG 8K, 10 MM DTT., pH 6.50	Resolution 2.50 Å R-free 0.291
1QUQ COMPLEX OF REPLICATION PROTEIN A SUBUNITS RPA14 AND RPA32 Deposited 1999-07-02	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 43–171（129 aa） Fragment：CENTRAL DOMAIN, RESIDUES 43-171	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；0.1 M MES, 0.75 M AMMONIUM SULPHATE, 20% PEG 8K, 10 MM DTT., pH 6.50	Resolution 2.50 Å R-free 0.291
1QUQ COMPLEX OF REPLICATION PROTEIN A SUBUNITS RPA14 AND RPA32 Deposited 1999-07-02	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 43–171（129 aa） Fragment：CENTRAL DOMAIN, RESIDUES 43-171	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；0.1 M MES, 0.75 M AMMONIUM SULPHATE, 20% PEG 8K, 10 MM DTT., pH 6.50	Resolution 2.50 Å R-free 0.291
1Z1D Structural Model for the interaction between RPA32 C-terminal domain and SV40 T antigen origin binding domain. Deposited 2005-03-03	Different construct Different mutation/modification 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 172–270（99 aa） Fragment：RPA32 C-terminal domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 0.03 M；Pressure ambient NMR sample composition 0.2mM RPA32C U-15N, 0.6mM Tag-OBD, 20mM Tris buffer pH 7.0, 2 mM DTT, 5mM MgCl2, 90% H2O, 10% D2O \| 90% H2O/10% D2O NMR sample composition 0.2mM Tag-OBD U-15N, 0.6mM RPA32C, 20mM Tris buffer pH 7.0, 2mM DTT, 5mM MgCl2, 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided
2PI2 Full-length Replication protein A subunits RPA14 and RPA32 Deposited 2007-04-12	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 1–270（270 aa）	Not recorded	DIO 1,4-DIETHYLENE DIOXIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；10% dioxane, 0.1 M MES pH 6.5, 39% saturated ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.00 Å R-free 0.255
2PI2 Full-length Replication protein A subunits RPA14 and RPA32 Deposited 2007-04-12	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–270（270 aa）	Not recorded	DIO 1,4-DIETHYLENE DIOXIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；10% dioxane, 0.1 M MES pH 6.5, 39% saturated ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.00 Å R-free 0.255
2PI2 Full-length Replication protein A subunits RPA14 and RPA32 Deposited 2007-04-12	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–270（270 aa）	Not recorded	DIO 1,4-DIETHYLENE DIOXIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；10% dioxane, 0.1 M MES pH 6.5, 39% saturated ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.00 Å R-free 0.255
2PI2 Full-length Replication protein A subunits RPA14 and RPA32 Deposited 2007-04-12	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–270（270 aa）	Not recorded	DIO 1,4-DIETHYLENE DIOXIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；10% dioxane, 0.1 M MES pH 6.5, 39% saturated ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.00 Å R-free 0.255
2PQA Crystal Structure of Full-length Human RPA 14/32 Heterodimer Deposited 2007-05-01	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 42–172（131 aa） Fragment：UNP residues 42-172	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；0.1 M Bicine pH 9, 20% saturated ammonium sulfate, 10% acetonitrile, VAPOR DIFFUSION, HANGING DROP, temperature 293K, pH 9.0	Resolution 2.50 Å R-free 0.280
2PQA Crystal Structure of Full-length Human RPA 14/32 Heterodimer Deposited 2007-05-01	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 42–172（131 aa） Fragment：UNP residues 42-172	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；0.1 M Bicine pH 9, 20% saturated ammonium sulfate, 10% acetonitrile, VAPOR DIFFUSION, HANGING DROP, temperature 293K, pH 9.0	Resolution 2.50 Å R-free 0.280
2Z6K Crystal structure of full-length human RPA14/32 heterodimer Deposited 2007-08-03	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 1–270（270 aa） Fragment：residues 42-175	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 5.9；293 K；0.95M KNa tartrate, 0.1M MES, 10mM DTT, pH 5.9, EVAPORATION, temperature 293K	Resolution 3.00 Å R-free 0.269
2Z6K Crystal structure of full-length human RPA14/32 heterodimer Deposited 2007-08-03	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–270（270 aa） Fragment：residues 42-175	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 5.9；293 K；0.95M KNa tartrate, 0.1M MES, 10mM DTT, pH 5.9, EVAPORATION, temperature 293K	Resolution 3.00 Å R-free 0.269
4MQV Crystal complex of Rpa32c and Smarcal1 N-terminus Deposited 2013-09-16	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 202–270（69 aa） Fragment：C-Terminal domain, UNP residues 202-270	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8；298 K；25% PEG 4000, 0.2M Sodium Acetate, pH 8.0, VAPOR DIFFUSION, temperature 298K	Resolution 1.95 Å R-free 0.220
4MQV Crystal complex of Rpa32c and Smarcal1 N-terminus Deposited 2013-09-16	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 202–270（69 aa） Fragment：C-Terminal domain, UNP residues 202-270	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8；298 K；25% PEG 4000, 0.2M Sodium Acetate, pH 8.0, VAPOR DIFFUSION, temperature 298K	Resolution 1.95 Å R-free 0.220
4OU0 Crystal Structure of RPA32C Deposited 2014-02-14	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 202–270（69 aa） Fragment：UNP RESIDUES 202-270	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；294 K；50 mM Sodium Acetate, 20% PEG 3350, pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 294K	Resolution 1.40 Å R-free 0.238
8RK2 Human Replication protein A (RPA; trimeric core) - ssDNA complex Deposited 2023-12-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–270（270 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
9MJ5 Catalytic domain of human DNA polymerase alpha in complex with DNA and RPA Deposited 2024-12-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 4 PDB declaration: hexameric	Chain B 35–270（236 aa）	Not recorded	ZN ZINC ION × 1 MG MAGNESIUM ION × 1 DCP 2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
9PD3 NER dual incision complex - DuIS Deposited 2025-06-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 15 PDB declaration: 17-meric	Chain O 1–270（270 aa）	Not recorded	SF4 IRON/SULFUR CLUSTER × 1 ZN ZINC ION × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
9PD4 NER dual incision complex - DuIM Deposited 2025-06-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 14 PDB declaration: hexadecameric	Chain O 1–270（270 aa）	Not recorded	SF4 IRON/SULFUR CLUSTER × 1 ZN ZINC ION × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å

13 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	RFA2_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–132； UniProt 41–172 Author chain D； PDBConstruct 1–132； UniProt 41–172

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	3kdf
Deposition date deposition_date	2009-10-22
Structure title title	X-ray Crystal Structure of the Human Replication Protein A Complex from Wheat Germ Cell Free Expression
Keywords keywords	;Wheat germ cell free, protein complex, Center for Eukaryotic Structural Genomics, PSI, replication protein A, Homo sapiens, Protein Structure Initiative, CESG, Acetylation, Alternative splicing, DNA replication, Nucleus, Phosphoprotein, Polymorphism, REPLICATION ;; REPLICATION
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	26.48 Å
Radius of gyration Rg (electron density) rg_electron	25.83 Å
Forward intensity I(0) i0	46842600.00
Molecular weight molecular_weight	53876.0 kDa
Excluded volume excluded_volume	67500 Å³
Envelope volume envelope_volume	81515 Å³
Hydration-shell volume shell_volume	26742 Å³
Envelope diameter envelope_diameter	89.4 Å
Shell Rg shell_rg	32.62 Å
Envelope Rg envelope_rg	26.09 Å
Shape Rg shape_rg	25.82 Å
Total Rg total_rg	26.60 Å
Total atoms total_atoms	3712
Residues n_residues	450
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	85.4 Å
Rg (real space) rg_real	26.49 Å
Rg uncertainty (real space) rg_real_error	0.52 Å
I(0) (real space) i0_real	4.6840e+07
I(0) uncertainty (real space) i0_real_error	6.6270e+05
Rg (reciprocal space) rg_reciprocal	26.49 Å
I(0) (reciprocal space) i0_reciprocal	46840000.0000
Solution quality estimate total_estimate	0.9000
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	27.1 Å
Skewness Skewness skewness	0.301
Kurtosis Kurtosis kurtosis	-0.529
Angular range angular_range	— – 0.3000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	13360000.0000
Real-space data points n_real_points	61
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.918; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.966; Smooth: 0.975

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Replication protein A 14 kDa subunit
Molecular weight formula_weight	13774.1 kDa
Mutation mutation	M1S
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C
Atom count atom_count	4185

SVDMMDLPRSRINAGMLAQFIDKPVCFVGRLEKIHPTGKMFILSDGEGKNGTIELMEPLDEEISGIVEVVGRVTAKATILCTSYVQFKEDSHPFDLGLYNEAVKIIHDFPQFYPLGIVQHD

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	cell-free synthesis

Entity 2 Entity 2 polymer

Description description	Replication protein A 32 kDa subunit
Molecular weight formula_weight	14982.4 kDa
Mutation mutation	A41S
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,B

SRAQHIVPCTISQLLSATLVDEVFRIGNVEISQVTIVGIIRHAEKAPTNIVYKIDDMTAAPMDVRQWVDTDDTSSENTVVPPETYVKVAGHLRSFQNKKSLVAFKIMPLEDMNEFTTHILEVINAHMVLSKA

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	cell-free synthesis

Entity 3 Entity 3 non-polymer

Description description	1,2-ETHANEDIOL
Molecular weight formula_weight	62.1 kDa
Source method src_method	syn
Copy count entity_count	7

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	258

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7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d3kdfa_
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.4 — Nucleic acid-binding proteins
Family Family family	b.40.4.3 — Single strand DNA-binding domain, SSB

Domain ID domain_id	d3kdfb_
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.4 — Nucleic acid-binding proteins
Family Family family	b.40.4.3 — Single strand DNA-binding domain, SSB

Domain ID domain_id	d3kdfc_
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.4 — Nucleic acid-binding proteins
Family Family family	b.40.4.3 — Single strand DNA-binding domain, SSB

Domain ID domain_id	d3kdfd_
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.4 — Nucleic acid-binding proteins
Family Family family	b.40.4.3 — Single strand DNA-binding domain, SSB

CATH v4.4 (4 domains)

Domain ID domain_id	3kdfA00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	140 — Nucleic acid-binding proteins

Domain ID domain_id	3kdfB00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	140 — Nucleic acid-binding proteins

Domain ID domain_id	3kdfC00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	140 — Nucleic acid-binding proteins

Domain ID domain_id	3kdfD00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	140 — Nucleic acid-binding proteins

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8. Citations (1)

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Unit-cell length a length_a	66.680 Å
Unit-cell length b length_b	77.700 Å
Unit-cell length c length_c	121.300 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	8

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

Resolution resolution	1.975 Å
Low-resolution limit resolution_low	36.999 Å
R factor r_factor	0.1920
R_work r_work	0.1920
R_free r_free	0.2060

fit	/app/data/saxs_computation/kd/3kdf/3kdf.fit
pddf	/app/data/pr_computation/kd/3kdf/3kdf.pr.out
profile	/app/data/saxs_computation/kd/3kdf/3kdf.dat

X-ray Crystal Structure of the Human Replication Protein A Complex from Wheat Germ Cell Free Expression

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

Replication protein A 14 kDa subunit

State in the Current Structure

Other States of the Same Protein in the Database

Replication protein A 32 kDa subunit

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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)