4Y18: BRCA1 BRCT domains

Structure of BRCA1 BRCT domains in complex with Abraxas double phosphorylated peptide. Determined by X-ray diffraction at 3.5 Å resolution. Released 27 Jan 2016.

Method: X-ray diffraction
Resolution: 3.5 Å
Organism: Homo sapiens
Chains: 16
Atoms: 13,976
Mol. weight: 217.64 kDa
Released: 27 Jan 2016

Explore 4Y18 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4Y18 contains 127 α-helices and 122 β-strands across 16 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, 18 β-strands

Element	Residues	Length	Sheet
β-strand	1649	1	1
β-strand	1651-1655	5	2
α-helix	1659-1671	13
β-strand	1675-1676	2	2
β-strand	1677	1	3
β-strand	1686-1689	4	2
β-strand	1691	1	4
β-strand	1696-1697	2	4
β-strand	1700	1	5
α-helix	1701-1708	8
β-strand	1712-1715	4	2
α-helix	1717-1725	9
α-helix	1731-1734	4
β-strand	1735	1	2
β-strand	1738-1739	2	4
β-strand	1743	1	4
α-helix	1748-1753	6
β-strand	1764-1768	5	6
α-helix	1777-1786	10
α-helix	1789	1
β-strand	1790-1791	2	6
α-helix	1795-1797	3
α-helix	1798-1800	3
β-strand	1805-1810	6	6
α-helix	1812-1814	3
α-helix	1820-1822	3
α-helix	1824-1826	3
β-strand	1832-1834	3	6
α-helix	1835-1844	10
α-helix	1850-1853	4
β-strand	1854	1	6
α-helix	1855-1856	2
β-strand	1857	1	7

Chain B: 15 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	1651-1655	5	8
α-helix	1659-1671	13
β-strand	1675-1676	2	8
β-strand	1677	1	3
β-strand	1686-1689	4	8
β-strand	1691	1	9
β-strand	1696-1697	2	9
α-helix	1701-1708	8
β-strand	1712-1715	4	8
α-helix	1717-1724	8
α-helix	1731-1734	4
β-strand	1735	1	8
β-strand	1738-1739	2	9
β-strand	1743	1	9
α-helix	1748-1754	7
β-strand	1764-1768	5	10
α-helix	1777-1786	10
α-helix	1789	1
β-strand	1790-1791	2	10
α-helix	1795-1797	3
α-helix	1798-1800	3
β-strand	1805-1810	6	10
α-helix	1812-1814	3
α-helix	1820-1822	3
α-helix	1824-1826	3
β-strand	1832-1834	3	10
α-helix	1835-1844	10
α-helix	1850-1853	4
β-strand	1854	1	10
α-helix	1855-1856	2
β-strand	1857	1	11

Chain C: 15 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	1649	1	11
β-strand	1651-1655	5	12
α-helix	1659-1671	13
β-strand	1675-1676	2	12
β-strand	1686-1689	4	12
β-strand	1691	1	13
β-strand	1696-1697	2	13
α-helix	1701-1708	8
β-strand	1712-1715	4	12
α-helix	1717-1725	9
α-helix	1731-1734	4
β-strand	1735	1	12
β-strand	1738-1739	2	13
β-strand	1743	1	13
α-helix	1748-1754	7
β-strand	1764-1768	5	14
α-helix	1777-1786	10
α-helix	1789	1
β-strand	1790-1791	2	14
α-helix	1795-1797	3
α-helix	1798-1800	3
β-strand	1805-1810	6	14
α-helix	1812-1814	3
α-helix	1820-1822	3
α-helix	1824-1826	3
β-strand	1832-1834	3	14
α-helix	1835-1844	10
α-helix	1850-1853	4
β-strand	1854	1	14
α-helix	1855-1856	2
β-strand	1857	1	15

Chain D: 15 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	1649	1	15
β-strand	1651-1655	5	16
α-helix	1659-1671	13
β-strand	1675-1676	2	16
β-strand	1686-1689	4	16
β-strand	1696-1697	2	17
α-helix	1701-1708	8
β-strand	1712-1715	4	16
α-helix	1717-1725	9
α-helix	1731-1734	4
β-strand	1735	1	16
β-strand	1738-1739	2	17
β-strand	1743	1	17
α-helix	1748-1754	7
α-helix	1756-1758	3
β-strand	1764-1768	5	18
α-helix	1777-1786	10
α-helix	1789	1
β-strand	1790-1791	2	18
α-helix	1795-1797	3
α-helix	1798-1800	3
β-strand	1805-1810	6	18
α-helix	1820-1822	3
α-helix	1824-1826	3
β-strand	1832-1834	3	18
α-helix	1835-1844	10
α-helix	1850-1853	4
β-strand	1854	1	18
α-helix	1855-1856	2

Chain E: 16 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	1651-1655	5	19
α-helix	1659-1672	14
β-strand	1675-1676	2	19
β-strand	1686-1689	4	19
β-strand	1691	1	20
β-strand	1696-1697	2	20
α-helix	1701-1708	8
β-strand	1712-1715	4	19
α-helix	1717-1724	8
α-helix	1731-1734	4
β-strand	1735	1	19
β-strand	1738-1739	2	20
β-strand	1743	1	20
α-helix	1748-1754	7
α-helix	1756-1758	3
β-strand	1765-1768	4	21
α-helix	1777-1786	10
α-helix	1789	1
β-strand	1790-1791	2	21
α-helix	1795-1797	3
α-helix	1798-1800	3
β-strand	1806-1810	5	21
α-helix	1812-1814	3
α-helix	1820-1822	3
α-helix	1824-1826	3
β-strand	1832-1834	3	21
α-helix	1835-1844	10
α-helix	1850-1853	4
β-strand	1854	1	21
α-helix	1855-1856	2
β-strand	1857	1	1

Chain F: 14 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	1649	1	7
β-strand	1651-1655	5	22
α-helix	1659-1671	13
β-strand	1675-1676	2	22
β-strand	1686-1689	4	22
β-strand	1696-1697	2	23
β-strand	1700	1	24
α-helix	1701-1708	8
β-strand	1712-1715	4	22
α-helix	1717-1725	9
α-helix	1731-1734	4
β-strand	1735	1	22
β-strand	1738-1739	2	23
β-strand	1743	1	23
α-helix	1748-1754	7
β-strand	1764-1769	6	25
α-helix	1777-1786	10
α-helix	1789	1
β-strand	1790-1792	3	25
α-helix	1795-1797	3
α-helix	1798-1800	3
β-strand	1805-1810	6	25
α-helix	1820-1822	3
α-helix	1824-1826	3
β-strand	1832-1834	3	25
α-helix	1835-1844	10
α-helix	1850-1853	4
β-strand	1854	1	25
α-helix	1855-1856	2

Chain G: 15 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	1651-1655	5	26
α-helix	1659-1671	13
β-strand	1675-1677	3	26
β-strand	1686-1689	4	26
β-strand	1696-1697	2	27
α-helix	1701-1708	8
β-strand	1712-1715	4	26
α-helix	1717-1725	9
α-helix	1731-1734	4
β-strand	1735	1	26
β-strand	1738-1739	2	27
β-strand	1743	1	27
α-helix	1748-1754	7
β-strand	1764-1768	5	28
α-helix	1777-1786	10
α-helix	1789	1
β-strand	1790-1791	2	28
α-helix	1795-1797	3
α-helix	1798-1800	3
β-strand	1805-1810	6	28
α-helix	1812-1814	3
α-helix	1820-1822	3
α-helix	1824-1827	4
β-strand	1832-1834	3	28
α-helix	1835-1844	10
α-helix	1850-1853	4
β-strand	1854	1	28
α-helix	1855-1856	2

Chain H: 15 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	1651-1655	5	26
α-helix	1659-1671	13
β-strand	1675-1677	3	26
β-strand	1686-1689	4	26
β-strand	1696-1697	2	29
α-helix	1701-1708	8
β-strand	1712-1715	4	26
α-helix	1717-1725	9
α-helix	1731-1734	4
β-strand	1735	1	26
β-strand	1738-1739	2	29
β-strand	1743	1	29
α-helix	1748-1754	7
β-strand	1764-1768	5	30
α-helix	1777-1786	10
α-helix	1789	1
β-strand	1790-1791	2	30
α-helix	1795-1797	3
α-helix	1798-1800	3
β-strand	1805-1810	6	30
α-helix	1812-1814	3
α-helix	1820-1822	3
α-helix	1824-1826	3
β-strand	1832-1834	3	30
α-helix	1835-1844	10
α-helix	1850-1853	4
β-strand	1854	1	30
α-helix	1855-1856	2

6 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Breast cancer type 1 susceptibility protein	A, B, C, D, E, F, G, H	protein	224	Homo sapiens	P38398 (AlphaFold model)
BRCA1-A complex subunit Abraxas	I, J, K, L, M, N, O, P	protein	11	Homo sapiens	Q6UWZ7 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA

>4Y18_1 Breast cancer type 1 susceptibility protein (chains A, B, C, D, E, F, G, H)
MSHHHHHHSMVNKRMSMVVSGLTPEEFMLVYKFARKHHITLTNLITEETTHVVMKTDAEF
VCERTLKYFLGIAGGKWVVSYFWVTQSIKERKMLNEHDFEVRGDVVNGRNHQGPKRARES
QDRKIFRGLEICCYGPFTNMPTDQLEWMVQLCGASVVKELSSFTLGTGVHPIVVVQPDAW
TEDNGFHAIGQMCEAPVVTREWVLDSVALYQCQELDTYLIPQIP

Sequence of entity 2 (I, J, K, L, M, N, O, P), FASTA

>4Y18_2 BRCA1-A complex subunit Abraxas (chains I, J, K, L, M, N, O, P)
GFGEYSRSPTF

Primary citation

Structure of BRCA1-BRCT/Abraxas Complex Reveals Phosphorylation-Dependent BRCT Dimerization at DNA Damage Sites. Wu, Q., Paul, A., Su, D. et al. Mol Cell (2016) 61:434-448. DOI 10.1016/j.molcel.2015.12.017 · PubMed

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

8RS8 1.31 Å, Crystal structure of BRCA1 BRCTs in complex with a RIF1 phosphopeptide
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…

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