2pi2

Full-length Replication protein A subunits RPA14 and RPA32

Method: X-RAY DIFFRACTION D_max: 112.3 Å Quality: GOOD

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

Replication protein A 32 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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–270	Not recorded	Replication protein A 14 kDa subunit × 1 （P35244） 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
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 1–270	Not recorded	Replication protein A 14 kDa subunit × 1 （P35244） 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
3	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 1–270	Not recorded	Replication protein A 14 kDa subunit × 1 （P35244） 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
4	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain D； UniProt 1–270	Not recorded	Replication protein A 14 kDa subunit × 1 （P35244） 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

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 2PI2	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 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 oligomeric state 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 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 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 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
2PQA Crystal Structure of Full-length Human RPA 14/32 Heterodimer Deposited 2007-05-01	Different construct 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 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 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 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
3KDF X-ray Crystal Structure of the Human Replication Protein A Complex from Wheat Germ Cell Free Expression Deposited 2009-10-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 41–172（132 aa） Fragment：Residues 41-172 Chain D 41–172（132 aa） Fragment：Residues 41-172	Mutation：A41S Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：A41S Non-standard monomer：Yes (specific site not provided by mmCIF)	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
3KDF X-ray Crystal Structure of the Human Replication Protein A Complex from Wheat Germ Cell Free Expression Deposited 2009-10-22	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 41–172（132 aa） Fragment：Residues 41-172	Mutation：A41S Non-standard monomer：Yes (specific site not provided by mmCIF)	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
3KDF X-ray Crystal Structure of the Human Replication Protein A Complex from Wheat Germ Cell Free Expression Deposited 2009-10-22	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 D 41–172（132 aa） Fragment：Residues 41-172	Mutation：A41S Non-standard monomer：Yes (specific site not provided by mmCIF)	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
4MQV Crystal complex of Rpa32c and Smarcal1 N-terminus Deposited 2013-09-16	Different construct 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 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 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 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 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 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 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	RFA2_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–270； UniProt 1–270 Author chain B； PDBConstruct 1–270； UniProt 1–270 Author chain C； PDBConstruct 1–270； UniProt 1–270 Author chain D； PDBConstruct 1–270； UniProt 1–270

Replication protein A 14 kDa subunit

Homo sapiens

UniProt P35244

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 E； UniProt 1–121	Not recorded	Replication protein A 32 kDa subunit × 1 （P15927） 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
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain F； UniProt 1–121	Not recorded	Replication protein A 32 kDa subunit × 1 （P15927） 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
3	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain G； UniProt 1–121	Not recorded	Replication protein A 32 kDa subunit × 1 （P15927） 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
4	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain H； UniProt 1–121	Not recorded	Replication protein A 32 kDa subunit × 1 （P15927） 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

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 2PI2	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 oligomeric state 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 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 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
2PQA Crystal Structure of Full-length Human RPA 14/32 Heterodimer Deposited 2007-05-01	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 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 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 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
3KDF X-ray Crystal Structure of the Human Replication Protein A Complex from Wheat Germ Cell Free Expression Deposited 2009-10-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–121（121 aa） Chain C 1–121（121 aa）	Mutation：M1S Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：M1S Non-standard monomer：Yes (specific site not provided by mmCIF)	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
3KDF X-ray Crystal Structure of the Human Replication Protein A Complex from Wheat Germ Cell Free Expression Deposited 2009-10-22	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–121（121 aa）	Mutation：M1S Non-standard monomer：Yes (specific site not provided by mmCIF)	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
3KDF X-ray Crystal Structure of the Human Replication Protein A Complex from Wheat Germ Cell Free Expression Deposited 2009-10-22	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 1–121（121 aa）	Mutation：M1S Non-standard monomer：Yes (specific site not provided by mmCIF)	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
8RK2 Human Replication protein A (RPA; trimeric core) - ssDNA complex Deposited 2023-12-22	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 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 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 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 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	RFA3_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain E； PDBConstruct 22–142； UniProt 1–121 Author chain F； PDBConstruct 22–142； UniProt 1–121 Author chain G； PDBConstruct 22–142； UniProt 1–121 Author chain H； PDBConstruct 22–142； UniProt 1–121

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	2pi2
Deposition date deposition_date	2007-04-12
Structure title title	Full-length Replication protein A subunits RPA14 and RPA32
Keywords keywords	full-length RPA14/32, ssDNA binding protein, OB-fold, Dioxane, REPLICATION, DNA BINDING PROTEIN; REPLICATION, DNA BINDING PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	37.45 Å
Radius of gyration Rg (electron density) rg_electron	36.99 Å
Forward intensity I(0) i0	169819000.00
Molecular weight molecular_weight	108790.0 kDa
Excluded volume excluded_volume	137870 Å³
Envelope volume envelope_volume	188560 Å³
Hydration-shell volume shell_volume	43594 Å³
Envelope diameter envelope_diameter	115.4 Å
Shell Rg shell_rg	42.28 Å
Envelope Rg envelope_rg	36.05 Å
Shape Rg shape_rg	37.00 Å
Total Rg total_rg	37.36 Å
Total atoms total_atoms	7636
Residues n_residues	972
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	112.3 Å
Rg (real space) rg_real	37.34 Å
Rg uncertainty (real space) rg_real_error	0.66 Å
I(0) (real space) i0_real	1.6980e+08
I(0) uncertainty (real space) i0_real_error	2.4690e+06
Rg (reciprocal space) rg_reciprocal	37.41 Å
I(0) (reciprocal space) i0_reciprocal	169800000.0000
Solution quality estimate total_estimate	0.8916
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	48.1 Å
Skewness Skewness skewness	0.097
Kurtosis Kurtosis kurtosis	-0.789
Angular range angular_range	— – 0.2100 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	15910000.0000
Real-space data points n_real_points	43
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.986; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.638

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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 32 kDa subunit
Molecular weight formula_weight	29276.8 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	7880

MWNSGFESYGSSSYGGAGGYTQSPGGFGSPAPSQAEKKSRARAQHIVPCTISQLLSATLVDEVFRIGNVEISQVTIVGIIRHAEKAPTNIVYKIDDMTAAPMDVRQWVDTDDTSSENTVVPPETYVKVAGHLRSFQNKKSLVAFKIMPLEDMNEFTTHILEVINAHMVLSKANSQPSAGRAPISNPGMSEAGNFGGNSFMPANGLTVAQNQVLNLIKACPRPEGLNFQDLKNQLKHMSVSSIKQAVDFLSNEGHIYSTVDDDHFKSTDAE

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	Replication protein A 14 kDa subunit
Molecular weight formula_weight	16117.5 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,F,G,H

MGHHHHHHHHHHSSGHIEGRHMVDMMDLPRSRINAGMLAQFIDKPVCFVGRLEKIHPTGKMFILSDGEGKNGTIELMEPLDEEISGIVEVVGRVTAKATILCTSYVQFKEDSHPFDLGLYNEAVKIIHDFPQFYPLGIVQHD

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 3 Entity 3 non-polymer

Description description	1,4-DIETHYLENE DIOXIDE
Molecular weight formula_weight	88.1 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	244

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7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d2pi2a_
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	d2pi2b_
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	d2pi2c_
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	d2pi2d_
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	d2pi2e_
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	d2pi2f_
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	d2pi2g_
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	d2pi2h_
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 (8 domains)

Domain ID domain_id	2pi2A00
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	2pi2B00
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	2pi2C00
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	2pi2D00
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	2pi2E00
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	2pi2F00
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	2pi2G00
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	2pi2H00
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	81.485 Å
Unit-cell length b length_b	139.826 Å
Unit-cell length c length_c	171.842 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	16

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

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.2332
R_work r_work	0.2321
R_free r_free	0.2549

fit	/app/data/saxs_computation/pi/2pi2/2pi2.fit
pddf	/app/data/pr_computation/pi/2pi2/2pi2.pr.out
profile	/app/data/saxs_computation/pi/2pi2/2pi2.dat

Full-length Replication protein A subunits RPA14 and RPA32

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

Replication protein A 32 kDa subunit

State in the Current Structure

Other States of the Same Protein in the Database

Replication protein A 14 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) 16 domains

SCOP 2.08 (8 domains)

CATH v4.4 (8 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)