ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Prion-like protein doppel

Intramolecular
Cysteine 94 and cysteine 145
Cysteine 108 and cysteine 140
Cysteine 94 and cysteine 108
Cysteine 8 and cysteine 14
Cysteine 140 and cysteine 145
Cysteine 108 and cysteine 145
Cysteine 94 and cysteine 140
A redox-regulated disulphide may form within Prion-like protein doppel between cysteines 94 and 145.

Details

Redox score ?
89
PDB code
1lg4
Structure name
nmr structure of the human doppel protein fragment 24-152
Structure deposition date
2002-04-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UKY0
Residue number A
94
Residue number B
145
Peptide name
Prion-like protein doppel

Ligandability

Cysteine 94 of Prion-like protein doppel

Cysteine 145 of Prion-like protein doppel

A redox-regulated disulphide may form within Prion-like protein doppel between cysteines 108 and 140.

Details

Redox score ?
83
PDB code
1lg4
Structure name
nmr structure of the human doppel protein fragment 24-152
Structure deposition date
2002-04-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UKY0
Residue number A
108
Residue number B
140
Peptide name
Prion-like protein doppel

Ligandability

Cysteine 108 of Prion-like protein doppel

Cysteine 140 of Prion-like protein doppel

A redox-regulated disulphide may form within Prion-like protein doppel between cysteines 94 and 108. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
1lg4
Structure name
nmr structure of the human doppel protein fragment 24-152
Structure deposition date
2002-04-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UKY0
Residue number A
94
Residue number B
108
Peptide name
Prion-like protein doppel

Ligandability

Cysteine 94 of Prion-like protein doppel

Cysteine 108 of Prion-like protein doppel

A redox-regulated disulphide may form within Prion-like protein doppel between cysteines 8 and 14. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
2m1j
Structure name
ovine doppel signal peptide (1-30)
Structure deposition date
2012-11-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
26
Minimum pKa ?
9
% buried
0
Peptide accession
Q9GJY2
Residue number A
8
Residue number B
14
Peptide name
Prion-like protein doppel

Ligandability

Cysteine 8 of Prion-like protein doppel

Cysteine 14 of Prion-like protein doppel

A redox-regulated disulphide may form within Prion-like protein doppel between cysteines 140 and 145. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
1lg4
Structure name
nmr structure of the human doppel protein fragment 24-152
Structure deposition date
2002-04-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UKY0
Residue number A
140
Residue number B
145
Peptide name
Prion-like protein doppel

Ligandability

Cysteine 140 of Prion-like protein doppel

Cysteine 145 of Prion-like protein doppel

A redox-regulated disulphide may form within Prion-like protein doppel between cysteines 108 and 145. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
1lg4
Structure name
nmr structure of the human doppel protein fragment 24-152
Structure deposition date
2002-04-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UKY0
Residue number A
108
Residue number B
145
Peptide name
Prion-like protein doppel

Ligandability

Cysteine 108 of Prion-like protein doppel

Cysteine 145 of Prion-like protein doppel

A redox-regulated disulphide may form within Prion-like protein doppel between cysteines 94 and 140. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
1lg4
Structure name
nmr structure of the human doppel protein fragment 24-152
Structure deposition date
2002-04-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UKY0
Residue number A
94
Residue number B
140
Peptide name
Prion-like protein doppel

Ligandability

Cysteine 94 of Prion-like protein doppel

Cysteine 140 of Prion-like protein doppel

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