2PQA: Full-length Human RPA 14/32 Heterodimer

Crystal Structure of Full-length Human RPA 14/32 Heterodimer. Determined by X-ray diffraction at 2.5 Å resolution. Released 13 Nov 2007.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,785
Mol. weight: 61.56 kDa
Released: 13 Nov 2007

Explore 2PQA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2PQA contains 16 α-helices and 30 β-strands across 4 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	90-95	6	1
α-helix	101	1
β-strand	102-106	5	1
α-helix	119-121	3
β-strand	125-135	11	1
β-strand	138-148	11	1
α-helix	153-171	19

Chain B: 6 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	10-12	3	3
α-helix	14-16	3
α-helix	18-20	3
β-strand	24-34	11	3
β-strand	40-44	5	3
β-strand	50-54	5	3
β-strand	66-73	8	3
α-helix	74	1
β-strand	79-86	8	3
α-helix	87-88	2
α-helix	96-108	13
α-helix	110-112	3

Chain C: 3 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	47-48	2	4
α-helix	51-55	5
β-strand	58-59	2	5
β-strand	64-66	3	5
β-strand	69-71	3	5
β-strand	73-85	13	4
β-strand	90-95	6	4
β-strand	102-106	5	4
α-helix	120-121	2
β-strand	125-134	10	4
β-strand	139-148	10	4
α-helix	153-169	17

Chain D: 3 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	10-12	3	6
α-helix	18-20	3
β-strand	24-34	11	6
β-strand	40-44	5	6
β-strand	50-54	5	6
β-strand	66-73	8	6
β-strand	79-86	8	6
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, C	protein	131	Homo sapiens	P15927 (AlphaFold model)
Replication protein A 14 kDa subunit	B, D	protein	142	Homo sapiens	P35244 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>2PQA_1 Replication protein A 32 kDa subunit (chains A, C)
RAQHIVPCTISQLLSATLVDEVFRIGNVEISQVTIVGIIRHAEKAPTNIVYKIDDMTAAP
MDVRQWVDTDDTSSENTVVPPETYVKVAGHLRSFQNKKSLVAFKIMPLEDMNEFTTHILE
VINAHMVLSKA

Sequence of entity 2 (B, D), FASTA

>2PQA_2 Replication protein A 14 kDa subunit (chains B, D)
MGHHHHHHHHHHSSGHIEGRHMVDMMDLPRSRINAGMLAQFIDKPVCFVGRLEKIHPTGK
MFILSDGEGKNGTIELMEPLDEEISGIVEVVGRVTAKATILCTSYVQFKEDSHPFDLGLY
NEAVKIIHDFPQFYPLGIVQHD

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…
2PI2 2.0 Å, Full-length Replication protein A subunits RPA14 and RPA32
1QUQ 2.5 Å, Complex of replication protein A subunits RPA14 and RPA32
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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