1QUQ: Protein

Complex of replication protein A subunits RPA14 and RPA32. Determined by X-ray diffraction at 2.5 Å resolution. Released 13 Aug 1999.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,786
Mol. weight: 56.03 kDa
Released: 13 Aug 1999

Explore 1QUQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1QUQ contains 16 α-helices and 29 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
α-helix	46	1
β-strand	47-48	2	1
α-helix	51-54	4
β-strand	58-59	2	2
β-strand	64-66	3	2
β-strand	69-71	3	2
β-strand	73-85	13	1
β-strand	89-95	7	1
β-strand	102-107	6	1
α-helix	119-121	3
β-strand	125-133	9	1
β-strand	140-148	9	1
α-helix	153-165	13

Chain B: 3 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	10-12	3	3
α-helix	14-19	6
β-strand	24-34	11	3
β-strand	40-44	5	3
β-strand	50-54	5	3
β-strand	66-73	8	3
β-strand	79-86	8	3
α-helix	96-108	13
α-helix	110-112	3

Chain C: 5 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	47-48	2	4
α-helix	51-55	5
β-strand	64-65	2	5
β-strand	70-71	2	5
β-strand	73-86	14	4
β-strand	89-95	7	4
α-helix	101	1
β-strand	102-107	6	4
α-helix	120-121	2
β-strand	125-135	11	4
β-strand	138-148	11	4
α-helix	149	1
α-helix	153-165	13

Chain D: 4 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	4-6	3
β-strand	10-12	3	6
α-helix	14-19	6
β-strand	24-34	11	6
β-strand	40-44	5	6
β-strand	50-55	6	6
β-strand	66-73	8	6
β-strand	79-86	8	6
α-helix	87-88	2
α-helix	96-108	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein (replication protein A 32 kd subunit)	A, C	protein	129	Homo sapiens	P15927 (AlphaFold model)
Protein (replication protein A 14 kd subunit)	B, D	protein	121	Homo sapiens	P35244 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>1QUQ_1 PROTEIN (REPLICATION PROTEIN A 32 KD SUBUNIT) (chains A, C)
AQHIVPCTISQLLSATLVDEVFRIGNVEISQVTIVGIIRHAEKAPTNIVYKIDDMTAAPM
DVRQWVDTDDTSSENTVVPPETYVKVAGHLRSFQNKKSLVAFKIMPLEDMNEFTTHILEV
INAHMVLSK

Sequence of entity 2 (B, D), FASTA

>1QUQ_2 PROTEIN (REPLICATION PROTEIN A 14 KD SUBUNIT) (chains B, D)
MVDMMDLPRSRINAGMLAQFIDKPVCFVGRLEKIHPTGKMFILSDGEGKNGTIELMEPLD
EEISGIVEVVGRVTAKATILCTSYVQFKEDSHPFDLGLYNEAVKIIHDFPQFYPLGIVQH
D

Primary citation

The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding. Bochkarev, A., Bochkareva, E., Frappier, L. et al. EMBO J (1999) 18:4498-4504. DOI 10.1093/emboj/18.16.4498 · 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
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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