1OA8: AXH domain of human spinocerebellar ataxin-1

AXH domain of human spinocerebellar ataxin-1. Determined by X-ray diffraction at 1.7 Å resolution. Released 6 Nov 2003.

Method: X-ray diffraction
Resolution: 1.7 Å
Organism: HOMO SAPIENS
Chains: 4
Atoms: 4,315
Mol. weight: 57.78 kDa
Released: 6 Nov 2003

Explore 1OA8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1OA8 contains 30 α-helices and 38 β-strands across 4 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: 8 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	564	1
β-strand	565-566	2	1
α-helix	567-568	2
α-helix	573-575	3
β-strand	580-582	3	2
β-strand	588-590	3	2
α-helix	591-593	3
α-helix	596-605	10
β-strand	609-621	13	1
β-strand	627-634	8	1
β-strand	639-646	8	1
α-helix	649-650	2
β-strand	651-653	3	1
β-strand	657-660	4	1
α-helix	663-670	8
β-strand	675-676	2	1
α-helix	677	1
β-strand	682-688	7	1

Chain B: 7 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	568-570	3
α-helix	574-576	3
β-strand	580-582	3	2
β-strand	588-590	3	2
α-helix	591-593	3
α-helix	596-598	3
β-strand	613-621	9	1
β-strand	627-634	8	1
β-strand	639-646	8	1
α-helix	649-650	2
β-strand	651-653	3	1
β-strand	657-660	4	1
α-helix	663-670	8
β-strand	675-676	2	1
α-helix	677	1
β-strand	682-684	3	1

Chain C: 7 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	565-566	2	3
α-helix	573-575	3
β-strand	580-582	3	4
β-strand	588-590	3	4
α-helix	591-593	3
α-helix	596-605	10
β-strand	609-621	13	3
β-strand	627-634	8	3
α-helix	636-638	3
β-strand	639-646	8	3
α-helix	649-650	2
β-strand	651-653	3	3
β-strand	657-660	4	3
α-helix	663-670	8
β-strand	675-676	2	3
α-helix	677	1
β-strand	682-688	7	3

Chain D: 8 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	564-566	3
α-helix	574-576	3
β-strand	580-582	3	4
α-helix	583	1
β-strand	588-590	3	4
α-helix	591-593	3
α-helix	596-605	10
β-strand	609-621	13	5
β-strand	627-634	8	5
β-strand	639-646	8	5
β-strand	651-653	3	5
β-strand	657-660	4	5
α-helix	663-670	8
β-strand	675-676	2	5
α-helix	677	1
β-strand	682-688	7	5
α-helix	689-691	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ataxin-1	A, B, C, D	protein	133	HOMO SAPIENS	P54253 (AlphaFold model)

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

>1OA8_1 ATAXIN-1 (chains A, B, C, D)
GSPAAAPPTLPPYFMKGSIIQLANGELKKVEDLKTEDFIQSAEISNDLKIDSSTVERIED
SHSPGVAVIQFAVGEHRAQVSVEVLVEYPFFVFGQGWSSCCPERTSQLFDLPCSKLSVGD
VCISLTLKNLKNG

Primary citation

The structure of the AXH domain of spinocerebellar ataxin-1. Chen, Y.W., Allen, M.D., Veprintsev, D.B. et al. J Biol Chem (2004) 279:3758-3765. DOI 10.1074/jbc.M309817200 · PubMed

Other PDB entries of the same protein (UniProt P54253 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6QIU 1.8 Å, Crystal structure of 14-3-3 sigma in complex with Ataxin-1 Ser776 phosphopeptide
4AQP 2.45 Å, The structure of the AXH domain of ataxin-1.
4APT 2.5 Å, The structure of the AXH domain of ataxin-1.
4J2J 2.5 Å, Crystal structure of AXH domain complex with Capicua
4J2L 3.15 Å, Crystal Structure of AXH domain complexed with Capicua
2M41 Solution Structure of the AXH domain of Ataxin-1 in complex with ligand peptide from…

Browse structure collections

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