Ataxin-3
2aga A 23 A 177
A redox-regulated disulphide may form within Ataxin-3 between cysteines 18 and 172 (23 and 177 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
2aga
Structure name
de-ubiquitinating function of ataxin-3: insights from the solution structure of the josephin domain
Structure deposition date
2005-07-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
75
Minimum pKa ?
10
% buried
82
Peptide accession
P54252
Residue number A
18
Residue number B
172
Peptide name
Ataxin-3
Ligandability
Cysteine 18 of Ataxin-3
Cysteine 172 of Ataxin-3
2jri A 14 A 18
A redox-regulated disulphide may form within Ataxin-3 between cysteines 14 and 18. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
2jri
Structure name
solution structure of the josephin domain of ataxin-3 in complex with ubiquitin molecule
Structure deposition date
2007-06-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
90
Minimum pKa ?
10
% buried
90
Peptide accession
P54252
Residue number A
14
Residue number B
18
Peptide name
Ataxin-3
Ligandability
Cysteine 14 of Ataxin-3
Cysteine 18 of Ataxin-3
2aga A 23 A 119
A redox-regulated disulphide may form within Ataxin-3 between cysteines 18 and 114 (23 and 119 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
2aga
Structure name
de-ubiquitinating function of ataxin-3: insights from the solution structure of the josephin domain
Structure deposition date
2005-07-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
11
% buried
96
Peptide accession
P54252
Residue number A
18
Residue number B
114
Peptide name
Ataxin-3
Ligandability
Cysteine 18 of Ataxin-3
Cysteine 114 of Ataxin-3
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