1N5O: Breast cancer type 1 susceptibility protein

Structural consequences of a cancer-causing BRCA1-BRCT missense mutation. Determined by X-ray diffraction at 2.8 Å resolution. Released 25 Dec 2002.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 1
Atoms: 1,618
Mol. weight: 24.81 kDa
Ligands: CO
Released: 25 Dec 2002

Explore 1N5O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1N5O contains 11 α-helices and 12 β-strands across 1 chain. 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 X: 11 helices, 12 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	1	2
α-helix	1701-1708	8
β-strand	1712-1715	4	1
α-helix	1717-1725	9
α-helix	1731-1734	4
β-strand	1735	1	1
β-strand	1738	1	2
α-helix	1748-1754	7
β-strand	1764-1768	5	3
α-helix	1777-1786	10
β-strand	1790-1792	3	3
α-helix	1795-1797	3
β-strand	1805-1810	6	3
α-helix	1812-1814	3
β-strand	1832-1834	3	3
α-helix	1836-1843	8
α-helix	1847-1849	3
α-helix	1850-1852	3
β-strand	1854	1	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Breast cancer type 1 susceptibility protein	X	protein	214	Homo sapiens	P38398 (AlphaFold model)

Sequence of entity 1 (X), FASTA

>1N5O_1 Breast cancer type 1 susceptibility protein (chains X)
VNKRMSMVVSGLTPEEFMLVYKFARKHHITLTNLITEETTHVVMKTDAEFVCERTLKYFL
GIAGGKWVVSYFWVTQSIKERKMLNEHDFEVRGDVVNGRNHQGPKRARESQDRKIFRGLE
ICCYGPFTNRPTDQLEWMVQLCGASVVKELSSFTLGTGVHPIVVVQPDAWTEDNGFHAIG
QMCEAPVVTREWVLDSVALYQCQELDTYLIPQIP

Ligands and cofactors

ID	Name	Formula	Copies
CO	Cobalt (II) ion	Co	1

Water and common crystallization additives (SO4) are not listed.

Primary citation

Structural consequences of a cancer-causing BRCA1-BRCT missense mutation. Williams, R.S., Glover, J.N.M. J Biol Chem (2003) 278:2630-2635. DOI 10.1074/jbc.M210019200 · 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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