2AGA: Machado-Joseph disease protein 1

De-ubiquitinating function of ataxin-3: insights from the solution structure of the Josephin domain. Determined by solution NMR. Released 30 Aug 2005.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
1,533
Mol. weight
21.82 kDa
Released
30 Aug 2005

Explore 2AGA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2AGA contains 8 α-helices and 6 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: 8 helices, 6 β-strands

ElementResiduesLengthSheet
α-helix5-84
α-helix21-277
α-helix35-5622
α-helix61-677
α-helix83-9210
β-strand95-9841
α-helix102-1087
β-strand116-12051
β-strand125-13171
β-strand134-13851
β-strand146-14831
α-helix150-16314
β-strand167-17151
α-helix178-1836

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Machado-Joseph disease protein 1Aprotein190Homo sapiensP54252 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2AGA_1 Machado-Joseph disease protein 1 (chains A)
GPLGSMESIFHEKQEGSLCAQHCLNNLLQGEYFSPVELSSIAHQLDEEERMRMAEGGVTS
EDYRTFLQQPSGNMDDSGFFSIQVISNALKVWGLELILFNSPEYQRLRIDPINERSFICN
YKEHWFTVRKLGKQWFNLNSLLTGPELISDTYLALFLAQLQQEGYSIFVVKGDLPDCEAD
QLLQMIRVQQ

Primary citation

Deubiquitinating function of ataxin-3: insights from the solution structure of the Josephin domain. Mao, Y., Senic-Matuglia, F., Di Fiore, P.P. et al. Proc Natl Acad Sci U S A (2005) 102:12700-12705. DOI 10.1073/pnas.0506344102 · PubMed

Other PDB entries of the same protein (UniProt P54252 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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