2PI2: Replication protein A 32 kDa subunit
Full-length Replication protein A subunits RPA14 and RPA32. Determined by X-ray diffraction at 2.0 Å resolution. Released 16 Oct 2007.
- Method
- X-ray diffraction
- Resolution
- 2.0 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 7,880
- Mol. weight
- 181.93 kDa
- Ligands
- DIO
- Released
- 16 Oct 2007
Explore 2PI2 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2PI2 contains 32 α-helices and 60 β-strands across 8 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
Chain A: 4 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 47-48 | 2 | 1 |
| α-helix | 51-56 | 6 | |
| β-strand | 58-60 | 3 | 2 |
| β-strand | 63-66 | 4 | 2 |
| β-strand | 69-71 | 3 | 2 |
| β-strand | 73-85 | 13 | 1 |
| β-strand | 89-95 | 7 | 1 |
| α-helix | 101 | 1 | |
| β-strand | 102-107 | 6 | 1 |
| α-helix | 118-121 | 4 | |
| β-strand | 125-135 | 11 | 1 |
| β-strand | 138-148 | 11 | 1 |
| α-helix | 153-172 | 20 | |
Chain B: 3 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 47-48 | 2 | 3 |
| α-helix | 51-55 | 5 | |
| β-strand | 58-59 | 2 | 4 |
| β-strand | 64-66 | 3 | 4 |
| β-strand | 69-71 | 3 | 4 |
| β-strand | 73-86 | 14 | 3 |
| β-strand | 89-95 | 7 | 3 |
| β-strand | 102-107 | 6 | 3 |
| α-helix | 119-121 | 3 | |
| β-strand | 125-135 | 11 | 3 |
| β-strand | 138-148 | 11 | 3 |
| α-helix | 153-173 | 21 | |
Chain C: 3 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 46-48 | 3 | 5 |
| α-helix | 51-55 | 5 | |
| β-strand | 58-59 | 2 | 6 |
| β-strand | 64-66 | 3 | 6 |
| β-strand | 69-71 | 3 | 6 |
| β-strand | 73-85 | 13 | 5 |
| β-strand | 89-95 | 7 | 5 |
| β-strand | 102-107 | 6 | 5 |
| α-helix | 118-121 | 4 | |
| β-strand | 125-133 | 9 | 5 |
| β-strand | 140-148 | 9 | 5 |
| α-helix | 153-172 | 20 | |
Chain D: 3 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 47-48 | 2 | 7 |
| α-helix | 51-56 | 6 | |
| β-strand | 58-60 | 3 | 8 |
| β-strand | 63-66 | 4 | 8 |
| β-strand | 69-71 | 3 | 8 |
| β-strand | 73-85 | 13 | 7 |
| β-strand | 89-95 | 7 | 7 |
| β-strand | 102-107 | 6 | 7 |
| α-helix | 119-121 | 3 | |
| β-strand | 125-134 | 10 | 7 |
| β-strand | 139-148 | 10 | 7 |
| α-helix | 153-172 | 20 | |
Chains E and G: 5 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-6 | 3 | |
| β-strand | 10-12 | 3 | 9 |
| α-helix | 14-19 | 6 | |
| β-strand | 24-34 | 11 | 9 |
| β-strand | 40-44 | 5 | 9 |
| β-strand | 50-54 | 5 | 9 |
| β-strand | 66-73 | 8 | 9 |
| β-strand | 79-86 | 8 | 9 |
| α-helix | 87-88 | 2 | |
| α-helix | 96-108 | 13 | |
| α-helix | 110-112 | 3 | |
Chain F: 5 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-6 | 3 | |
| β-strand | 10-12 | 3 | 10 |
| α-helix | 14-19 | 6 | |
| β-strand | 24-34 | 11 | 10 |
| β-strand | 40-44 | 5 | 10 |
| β-strand | 50-55 | 6 | 10 |
| β-strand | 66-73 | 8 | 10 |
| β-strand | 79-86 | 8 | 10 |
| α-helix | 87-88 | 2 | |
| α-helix | 96-108 | 13 | |
| α-helix | 110-112 | 3 | |
Chain H: 4 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 10-12 | 3 | 12 |
| α-helix | 14-19 | 6 | |
| β-strand | 24-34 | 11 | 12 |
| β-strand | 40-44 | 5 | 12 |
| β-strand | 50-55 | 6 | 12 |
| β-strand | 66-73 | 8 | 12 |
| β-strand | 79-86 | 8 | 12 |
| α-helix | 87-88 | 2 | |
| α-helix | 96-108 | 13 | |
| α-helix | 110-112 | 3 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Replication protein A 32 kDa subunit | A, B, C, D | protein | 270 | Homo sapiens | P15927 (AlphaFold model) |
| Replication protein A 14 kDa subunit | E, F, G, H | protein | 142 | Homo sapiens | P35244 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D), FASTA
>2PI2_1 Replication protein A 32 kDa subunit (chains A, B, C, D)
MWNSGFESYGSSSYGGAGGYTQSPGGFGSPAPSQAEKKSRARAQHIVPCTISQLLSATLV
DEVFRIGNVEISQVTIVGIIRHAEKAPTNIVYKIDDMTAAPMDVRQWVDTDDTSSENTVV
PPETYVKVAGHLRSFQNKKSLVAFKIMPLEDMNEFTTHILEVINAHMVLSKANSQPSAGR
APISNPGMSEAGNFGGNSFMPANGLTVAQNQVLNLIKACPRPEGLNFQDLKNQLKHMSVS
SIKQAVDFLSNEGHIYSTVDDDHFKSTDAE
Sequence of entity 2 (E, F, G, H), FASTA
>2PI2_2 Replication protein A 14 kDa subunit (chains E, F, G, H)
MGHHHHHHHHHHSSGHIEGRHMVDMMDLPRSRINAGMLAQFIDKPVCFVGRLEKIHPTGK
MFILSDGEGKNGTIELMEPLDEEISGIVEVVGRVTAKATILCTSYVQFKEDSHPFDLGLY
NEAVKIIHDFPQFYPLGIVQHD
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| DIO | 1,4-diethylene dioxide | C4 H8 O2 | 4 |
Primary citation
Structure of the Full-length Human RPA14/32 Complex Gives Insights into the Mechanism of DNA Binding and Complex Formation. Deng, X., Habel, J.E., Kabaleeswaran, V. et al. J Mol Biol (2007) 374:865-876. DOI 10.1016/j.jmb.2007.09.074 · PubMed
Other PDB entries of the same protein (UniProt P15927 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 4OU0 1.4 Å, Crystal Structure of RPA32C
- 4MQV 1.95 Å, Crystal complex of Rpa32c and Smarcal1 N-terminus
- 3KDF 1.98 Å, X-ray Crystal Structure of the Human Replication Protein A Complex from Wheat Germ Cell…
- 1QUQ 2.5 Å, Complex of replication protein A subunits RPA14 and RPA32
- 2PQA 2.5 Å, Crystal Structure of Full-length Human RPA 14/32 Heterodimer
- 1L1O 2.8 Å, Structure of the human Replication Protein A (RPA) trimerization core
- 2Z6K 3.0 Å, Crystal structure of full-length human RPA14/32 heterodimer
- 8RK2 3.2 Å, Human Replication protein A (RPA; trimeric core) - ssDNA complex
- 9PD3 3.3 Å, NER dual incision complex - DuIS
- 9PD4 3.4 Å, NER dual incision complex - DuIM
- 9MJ5 3.5 Å, Catalytic domain of human DNA polymerase alpha in complex with DNA and RPA
- 1DPU Solution structure of the C-terminal domain of human RPA32 complexed with UNG2(73-88)
Browse structure collections
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