3PXA: Breast cancer type 1 susceptibility protein

Impact of BRCA1 BRCT domain missense substitutions on phospho-peptide recognition: G1656D. Determined by X-ray diffraction at 2.55 Å resolution. Released 20 Apr 2011.

Method: X-ray diffraction
Resolution: 2.55 Å
Organism: Homo sapiens
Chains: 1
Atoms: 1,665
Mol. weight: 24.74 kDa
Ligands: NI
Released: 20 Apr 2011

Explore 3PXA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3PXA contains 12 α-helices and 13 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 A: 12 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	1651-1655	5	1
α-helix	1659-1672	14
β-strand	1675-1676	2	1
β-strand	1686-1689	4	1
β-strand	1691	1	2
β-strand	1696-1697	2	2
α-helix	1701-1708	8
β-strand	1712-1715	4	1
α-helix	1717-1724	8
α-helix	1731-1734	4
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	3
α-helix	1777-1786	10
β-strand	1789-1791	3	3
α-helix	1795-1797	3
β-strand	1805-1810	6	3
α-helix	1812-1814	3
α-helix	1824-1826	3
β-strand	1832-1834	3	3
α-helix	1835-1843	9
α-helix	1850-1852	3
α-helix	1854-1856	3

Molecules and chains

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

Sequence of entity 1 (A), FASTA

>3PXA_1 Breast cancer type 1 susceptibility protein (chains A)
VNKRMSMVVSDLTPEEFMLVYKFARKHHITLTNLITEETTHVVMKTDAEFVCERTLKYFL
GIAGGKWVVSYFWVTQSIKERKMLNEHDFEVRGDVVNGRNHQGPKRARESQDRKIFRGLE
ICCYGPFTNMPTDQLEWMVQLCGASVVKELSSFTLGTGVHPIVVVQPDAWTEDNGFHAIG
QMCEAPVVTREWVLDSVALYQCQELDTYLIPQIP

Ligands and cofactors

ID	Name	Formula	Copies
NI	Nickel (II) ion	Ni	1

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

Primary citation

Impact of BRCA1 BRCT Domain Missense Substitutions on Phosphopeptide Recognition. Coquelle, N., Green, R., Glover, J.N. Biochemistry (2011) 50:4579-4589. DOI 10.1021/bi2003795 · 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
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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