1L1O: Replication protein A 14 kDa subunit

Structure of the human Replication Protein A (RPA) trimerization core. Determined by X-ray diffraction at 2.8 Å resolution. Released 5 Jun 2002.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 6
Atoms: 6,569
Mol. weight: 98.31 kDa
Ligands: ZN
Released: 5 Jun 2002

Explore 1L1O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1L1O contains 27 α-helices and 58 β-strands across 6 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: 3 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	10-12	3	1
α-helix	14-16	3
β-strand	24-34	11	1
β-strand	40-44	5	1
β-strand	50-55	6	1
β-strand	66-73	8	1
β-strand	79-86	8	1
α-helix	96-108	13
α-helix	110-112	3

Chain B: 4 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	46-48	3	2
α-helix	51-56	6
β-strand	58	1	3
β-strand	65-66	2	3
β-strand	69-70	2	3
β-strand	73-84	12	2
β-strand	89-95	7	2
α-helix	101	1
β-strand	102-107	6	2
α-helix	119-121	3
β-strand	125-135	11	2
β-strand	138-145	8	2
β-strand	148	1	2
α-helix	153-169	17

Chain C: 7 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	442	1	4
α-helix	445-451	7
β-strand	460-471	12	4
β-strand	477-479	3	5
β-strand	480	1	6
α-helix	488	1
β-strand	489	1	6
α-helix	490	1
β-strand	491-493	3	7
β-strand	497-500	4	7
β-strand	505-507	3	7
β-strand	512-514	3	5
β-strand	515-521	7	4
β-strand	526-532	7	4
α-helix	533-540	8
α-helix	544-550	7
α-helix	555-564	10
β-strand	569-577	9	4
β-strand	588-596	9	4
α-helix	599-615	17

Chain D: 4 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	4-6	3
β-strand	10-12	3	8
α-helix	14-20	7
β-strand	24-31	8	8
β-strand	40-44	5	8
β-strand	50-54	5	8
β-strand	66-73	8	8
β-strand	79-86	8	8
α-helix	96-108	13
α-helix	110-112	3

Chain E: 4 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	46-48	3	9
α-helix	51-56	6
β-strand	58	1	10
β-strand	65-66	2	10
β-strand	69-70	2	10
β-strand	73-85	13	9
β-strand	90-95	6	9
α-helix	101	1
β-strand	102-106	5	9
α-helix	119-121	3
β-strand	125-133	9	9
β-strand	140-142	3	9
β-strand	147-148	2	9
α-helix	153-170	18

Chain F: 5 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	442	1	11
α-helix	445-450	6
β-strand	461-472	12	11
β-strand	477-479	3	12
β-strand	480	1	13
β-strand	489	1	13
β-strand	491-492	2	14
β-strand	498-500	3	14
β-strand	505-507	3	14
β-strand	512-514	3	12
β-strand	515-521	7	11
β-strand	526-532	7	11
α-helix	533-540	8
α-helix	544-553	10
α-helix	555-564	10
β-strand	569-577	9	11
β-strand	588-596	9	11
α-helix	599-614	16

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Replication protein A 14 kDa subunit	A, D	protein	121	Homo sapiens	P35244 (AlphaFold model)
Replication protein A 32 kDa subunit	B, E	protein	128	Homo sapiens	P15927 (AlphaFold model)
Replication protein A 70 kDa DNA-binding subunit	C, F	protein	181	Homo sapiens	P27694 (AlphaFold model)

Sequence of entity 1 (A, D), FASTA

>1L1O_1 Replication protein A 14 kDa subunit (chains A, D)
MVDMMDLPRSRINAGMLAQFIDKPVCFVGRLEKIHPTGKMFILSDGEGKNGTIELMEPLD
EEISGIVEVVGRVTAKATILCTSYVQFKEDSHPFDLGLYNEAVKIIHDFPQFYPLGIVQH
D

Sequence of entity 2 (B, E), FASTA

>1L1O_2 Replication protein A 32 kDa subunit (chains B, E)
QHIVPCTISQLLSATLVDEVFRIGNVEISQVTIVGIIRHAEKAPTNIVYKIDDMTAAPMD
VRQWVDTDDTSSENTVVPPETYVKVAGHLRSFQNKKSLVAFKIMPLEDMNEFTTHILEVI
NAHMVLSK

Sequence of entity 3 (C, F), FASTA

>1L1O_3 Replication protein A 70 kDa DNA-binding subunit (chains C, F)
GGSNTNWKTLYEVKSENLGQGDKPDYFSSVATVVYLRKENCMYQACPTQDCNKKVIDQQN
GLYRCEKCDTEFPNFKYRMILSVNIADFQENQWVTCFQESAEAILGQNAAYLGELKDKNE
QAFEEVFQNANFRSFIFRVRVKVETYNDESRIKATVMDVKPVDYREYGRRLVMSIRRSAL
M

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	2

Primary citation

Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA. Bochkareva, E., Korolev, S., Lees-Miller, S.P. et al. EMBO J (2002) 21:1855-1863. DOI 10.1093/emboj/21.7.1855 · PubMed

Other PDB entries of the same protein (UniProt P35244 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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
2PQA 2.5 Å, Crystal Structure of Full-length Human RPA 14/32 Heterodimer
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
9A1V Integrative model of Nucleotide excision repair complex of XPA and RPA on 5' junction…
9A1Y Integrative model of Nucleotide excision repair complex of XPA and RPA on 3' junction…
9A88 Structure of the pre-incision complex in nucleotide excision repair

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