8RS8: BRCA1 BRCTs

Crystal structure of BRCA1 BRCTs in complex with a RIF1 phosphopeptide. Determined by X-ray diffraction at 1.31 Å resolution. Released 16 Jul 2025.

Method: X-ray diffraction
Resolution: 1.31 Å
Organism: Homo sapiens
Chains: 8
Atoms: 8,484
Mol. weight: 106.67 kDa
Released: 16 Jul 2025

Explore 8RS8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8RS8 contains 58 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: 15 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	1651-1655	5	1
α-helix	1659-1671	13
β-strand	1675-1676	2	1
β-strand	1686-1689	4	1
β-strand	1696-1697	2	2
β-strand	1700	1	3
α-helix	1701-1708	8
β-strand	1712-1715	4	1
α-helix	1717-1725	9
α-helix	1728-1730	3
α-helix	1731-1733	3
β-strand	1735	1	1
β-strand	1738-1739	2	2
β-strand	1743	1	2
α-helix	1748-1754	7
β-strand	1764-1768	5	4
α-helix	1777-1786	10
β-strand	1790-1792	3	4
α-helix	1795-1797	3
β-strand	1805-1810	6	4
α-helix	1812-1815	4
α-helix	1819-1822	4
α-helix	1824-1826	3
β-strand	1832-1834	3	4
α-helix	1835-1844	10
α-helix	1847-1849	3
α-helix	1851-1853	3
β-strand	1854	1	4
α-helix	1855-1856	2

Chain B: 14 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	1651-1655	5	5
α-helix	1659-1672	14
β-strand	1675-1676	2	5
β-strand	1686-1689	4	5
β-strand	1696-1697	2	6
β-strand	1700	1	7
α-helix	1701-1708	8
β-strand	1712-1715	4	5
α-helix	1717-1725	9
α-helix	1731-1734	4
β-strand	1735	1	5
β-strand	1738-1739	2	6
β-strand	1743	1	6
α-helix	1748-1754	7
β-strand	1765-1768	4	8
α-helix	1777-1786	10
α-helix	1789	1
β-strand	1790-1791	2	8
α-helix	1795-1797	3
β-strand	1806-1810	5	8
α-helix	1812-1815	4
α-helix	1820-1822	3
α-helix	1824-1826	3
β-strand	1832-1834	3	8
α-helix	1835-1844	10
α-helix	1847-1849	3
α-helix	1851-1853	3
β-strand	1854	1	8

Chain C: 14 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	1651-1655	5	9
α-helix	1659-1672	14
β-strand	1675-1676	2	9
β-strand	1686-1689	4	9
β-strand	1696-1697	2	10
β-strand	1700	1	11
α-helix	1701-1708	8
β-strand	1712-1715	4	9
α-helix	1717-1725	9
α-helix	1731-1734	4
β-strand	1735	1	9
β-strand	1738-1739	2	10
β-strand	1743	1	10
α-helix	1748-1754	7
β-strand	1764-1768	5	12
α-helix	1777-1786	10
α-helix	1789	1
β-strand	1790-1792	3	12
α-helix	1795-1797	3
β-strand	1805-1810	6	12
α-helix	1812-1814	3
α-helix	1820-1822	3
α-helix	1824-1826	3
β-strand	1832-1834	3	12
α-helix	1835-1844	10
α-helix	1851-1853	3
β-strand	1854	1	12
α-helix	1855-1858	4

Chain D: 15 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	1651-1655	5	13
α-helix	1659-1671	13
β-strand	1675-1676	2	13
β-strand	1686-1689	4	13
β-strand	1696-1697	2	14
β-strand	1700	1	15
α-helix	1701-1708	8
β-strand	1712-1715	4	13
α-helix	1717-1725	9
α-helix	1728-1730	3
α-helix	1731-1734	4
β-strand	1735	1	13
β-strand	1738-1739	2	14
β-strand	1743	1	14
α-helix	1748-1754	7
β-strand	1764-1768	5	16
α-helix	1777-1786	10
β-strand	1790-1791	2	16
α-helix	1795-1797	3
β-strand	1805-1810	6	16
α-helix	1812-1814	3
α-helix	1820-1822	3
α-helix	1824-1826	3
β-strand	1832-1834	3	16
α-helix	1835-1844	10
α-helix	1847-1849	3
α-helix	1851-1853	3
β-strand	1854	1	16
α-helix	1855-1856	2

Chains E, F, G and H: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	2267	1	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Breast cancer type 1 susceptibility protein	A, B, C, D	protein	217	Homo sapiens	P38398 (AlphaFold model)
Telomere-associated protein RIF1	E, F, G, H	protein	11	Homo sapiens	Q5UIP0 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>8RS8_1 Breast cancer type 1 susceptibility protein (chains A, B, C, D)
GPSVNKRMSMVVSGLTPEEFMLVYKFARKHHITLTNLITEETTHVVMKTDAEFVCERTLK
YFLGIAGGKWVVSYFWVTQSIKERKMLNEHDFEVRGDVVNGRNHQGPKRARESQDRKIFR
GLEICCYGPFTNMPTDQLEWMVQLCGASVVKELSSFTLGTGVHPIVVVQPDAWTEDNGFH
AIGQMCEAPVVTREWVLDSVALYQCQELDTYLIPQIP

Sequence of entity 2 (E, F, G, H), FASTA

>8RS8_2 Telomere-associated protein RIF1 (chains E, F, G, H)
SPGSRSPKFKS

Primary citation

The human RIF1-Long isoform interacts with BRCA1 to promote recombinational fork repair under DNA replication stress. Dong, Q., Day, M., Saito, Y. et al. Nat Commun (2025) 16:5820-5820. DOI 10.1038/s41467-025-60817-y · PubMed

Other PDB entries of the same protein (UniProt P38398 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4IGK 1.75 Å, Structure of human BRCA1 BRCT in complex with ATRIP peptide
1T15 1.85 Å, Crystal Structure of the Brca1 BRCT Domains in Complex with the Phosphorylated…
4IFI 2.2 Å, Structure of human BRCA1 BRCT in complex with BAAT peptide
1T29 2.3 Å, Crystal structure of the BRCA1 BRCT repeats bound to a phosphorylated BACH1 peptide
1JNX 2.5 Å, Crystal structure of the BRCT repeat region from the breast cancer associated protein,…
1Y98 2.5 Å, Structure of the BRCT repeats of BRCA1 bound to a CtIP phosphopeptide.
3PXB 2.5 Å, Impact of BRCA1 BRCT domain missense substitutions on phospho-peptide recognition: T1700A
4Y2G 2.5 Å, Structure of BRCA1 BRCT domains in complex with Abraxas single phosphorylated peptide
3PXA 2.55 Å, Impact of BRCA1 BRCT domain missense substitutions on phospho-peptide recognition: G1656D
3K0H 2.7 Å, The crystal structure of BRCA1 BRCT in complex with a minimal recognition tetrapeptide…
3K0K 2.7 Å, Crystal Structure of BRCA1 BRCT in complex with a minimal recognition tetrapeptide with…
1N5O 2.8 Å, Structural consequences of a cancer-causing BRCA1-BRCT missense mutation

Browse structure collections

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