← Back to search

Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：P15927 New Search
14PDB entries
24Biological assembly
27chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
1DPU SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF HUMAN RPA32 COMPLEXED WITH UNG2(73-88) Deposited 1999-12-27 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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 Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
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 Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
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 Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
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 Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
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 Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
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 Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
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 Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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 Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
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 Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
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 Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
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 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
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 Assembly 1 Protein–DNA Heteromer；Protein × 4 PDB declaration: hexameric（6） Consistent with all polymers
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 Assembly 1 Protein–DNA Heteromer；Protein × 15 PDB declaration: 17-meric（17） Consistent with all polymers
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 Assembly 1 Protein–DNA Heteromer；Protein × 14 PDB declaration: hexadecameric（16） Consistent with all polymers
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

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.