ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Peroxisome proliferator-activated receptor delta

Intramolecular
Cysteine 111 and cysteine 125
Cysteine 111 and cysteine 115
Cysteine 115 and cysteine 125
Cysteine 74 and cysteine 77
Cysteine 74 and cysteine 91
Cysteine 74 and cysteine 94
Cysteine 111 and cysteine 128
Cysteine 125 and cysteine 128
Cysteine 115 and cysteine 128
Cysteine 91 and cysteine 94
More...
Cysteine 77 and cysteine 91
Cysteine 77 and cysteine 94
Cysteine 74 and cysteine 133
Cysteine 94 and cysteine 133
Cysteine 91 and cysteine 133
Cysteine 77 and cysteine 133
Cysteine 249 and cysteine 251 L
A redox-regulated disulphide may form within Peroxisome proliferator-activated receptor delta between cysteines 111 and 125.

Details

Redox score ?
88
PDB code
2env
Structure name
solution structure of the c4-type zinc finger domain from human peroxisome proliferator-activated receptor delta
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
7
% buried
0
Peptide accession
Q03181
Residue number A
111
Residue number B
125
Peptide name
Peroxisome proliferator-activated receptor delta

Ligandability

Cysteine 111 of Peroxisome proliferator-activated receptor delta

Cysteine 125 of Peroxisome proliferator-activated receptor delta

A redox-regulated disulphide may form within Peroxisome proliferator-activated receptor delta between cysteines 111 and 115.

Details

Redox score ?
87
PDB code
2env
Structure name
solution structure of the c4-type zinc finger domain from human peroxisome proliferator-activated receptor delta
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
8
% buried
0
Peptide accession
Q03181
Residue number A
111
Residue number B
115
Peptide name
Peroxisome proliferator-activated receptor delta

Ligandability

Cysteine 111 of Peroxisome proliferator-activated receptor delta

Cysteine 115 of Peroxisome proliferator-activated receptor delta

A redox-regulated disulphide may form within Peroxisome proliferator-activated receptor delta between cysteines 115 and 125.

Details

Redox score ?
85
PDB code
2env
Structure name
solution structure of the c4-type zinc finger domain from human peroxisome proliferator-activated receptor delta
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
7
% buried
0
Peptide accession
Q03181
Residue number A
115
Residue number B
125
Peptide name
Peroxisome proliferator-activated receptor delta

Ligandability

Cysteine 115 of Peroxisome proliferator-activated receptor delta

Cysteine 125 of Peroxisome proliferator-activated receptor delta

A redox-regulated disulphide may form within Peroxisome proliferator-activated receptor delta between cysteines 74 and 77.

Details

Redox score ?
85
PDB code
2env
Structure name
solution structure of the c4-type zinc finger domain from human peroxisome proliferator-activated receptor delta
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
5
% buried
34
Peptide accession
Q03181
Residue number A
74
Residue number B
77
Peptide name
Peroxisome proliferator-activated receptor delta

Ligandability

Cysteine 74 of Peroxisome proliferator-activated receptor delta

Cysteine 77 of Peroxisome proliferator-activated receptor delta

A redox-regulated disulphide may form within Peroxisome proliferator-activated receptor delta between cysteines 74 and 91.

Details

Redox score ?
85
PDB code
2env
Structure name
solution structure of the c4-type zinc finger domain from human peroxisome proliferator-activated receptor delta
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
5
% buried
32
Peptide accession
Q03181
Residue number A
74
Residue number B
91
Peptide name
Peroxisome proliferator-activated receptor delta

Ligandability

Cysteine 74 of Peroxisome proliferator-activated receptor delta

Cysteine 91 of Peroxisome proliferator-activated receptor delta

A redox-regulated disulphide may form within Peroxisome proliferator-activated receptor delta between cysteines 74 and 94.

Details

Redox score ?
84
PDB code
2env
Structure name
solution structure of the c4-type zinc finger domain from human peroxisome proliferator-activated receptor delta
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
5
% buried
45
Peptide accession
Q03181
Residue number A
74
Residue number B
94
Peptide name
Peroxisome proliferator-activated receptor delta

Ligandability

Cysteine 74 of Peroxisome proliferator-activated receptor delta

Cysteine 94 of Peroxisome proliferator-activated receptor delta

A redox-regulated disulphide may form within Peroxisome proliferator-activated receptor delta between cysteines 111 and 128.

Details

Redox score ?
84
PDB code
2env
Structure name
solution structure of the c4-type zinc finger domain from human peroxisome proliferator-activated receptor delta
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
8
% buried
0
Peptide accession
Q03181
Residue number A
111
Residue number B
128
Peptide name
Peroxisome proliferator-activated receptor delta

Ligandability

Cysteine 111 of Peroxisome proliferator-activated receptor delta

Cysteine 128 of Peroxisome proliferator-activated receptor delta

A redox-regulated disulphide may form within Peroxisome proliferator-activated receptor delta between cysteines 125 and 128.

Details

Redox score ?
84
PDB code
2env
Structure name
solution structure of the c4-type zinc finger domain from human peroxisome proliferator-activated receptor delta
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
7
% buried
0
Peptide accession
Q03181
Residue number A
125
Residue number B
128
Peptide name
Peroxisome proliferator-activated receptor delta

Ligandability

Cysteine 125 of Peroxisome proliferator-activated receptor delta

Cysteine 128 of Peroxisome proliferator-activated receptor delta

A redox-regulated disulphide may form within Peroxisome proliferator-activated receptor delta between cysteines 115 and 128.

Details

Redox score ?
79
PDB code
2env
Structure name
solution structure of the c4-type zinc finger domain from human peroxisome proliferator-activated receptor delta
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
9
% buried
0
Peptide accession
Q03181
Residue number A
115
Residue number B
128
Peptide name
Peroxisome proliferator-activated receptor delta

Ligandability

Cysteine 115 of Peroxisome proliferator-activated receptor delta

Cysteine 128 of Peroxisome proliferator-activated receptor delta

A redox-regulated disulphide may form within Peroxisome proliferator-activated receptor delta between cysteines 91 and 94.

Details

Redox score ?
77
PDB code
2env
Structure name
solution structure of the c4-type zinc finger domain from human peroxisome proliferator-activated receptor delta
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
8
% buried
40
Peptide accession
Q03181
Residue number A
91
Residue number B
94
Peptide name
Peroxisome proliferator-activated receptor delta

Ligandability

Cysteine 91 of Peroxisome proliferator-activated receptor delta

Cysteine 94 of Peroxisome proliferator-activated receptor delta

A redox-regulated disulphide may form within Peroxisome proliferator-activated receptor delta between cysteines 77 and 91.

Details

Redox score ?
77
PDB code
2env
Structure name
solution structure of the c4-type zinc finger domain from human peroxisome proliferator-activated receptor delta
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
8
% buried
28
Peptide accession
Q03181
Residue number A
77
Residue number B
91
Peptide name
Peroxisome proliferator-activated receptor delta

Ligandability

Cysteine 77 of Peroxisome proliferator-activated receptor delta

Cysteine 91 of Peroxisome proliferator-activated receptor delta

A redox-regulated disulphide may form within Peroxisome proliferator-activated receptor delta between cysteines 77 and 94.

Details

Redox score ?
74
PDB code
2env
Structure name
solution structure of the c4-type zinc finger domain from human peroxisome proliferator-activated receptor delta
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
10
% buried
42
Peptide accession
Q03181
Residue number A
77
Residue number B
94
Peptide name
Peroxisome proliferator-activated receptor delta

Ligandability

Cysteine 77 of Peroxisome proliferator-activated receptor delta

Cysteine 94 of Peroxisome proliferator-activated receptor delta

A redox-regulated disulphide may form within Peroxisome proliferator-activated receptor delta between cysteines 74 and 133.

Details

Redox score ?
61
PDB code
2env
Structure name
solution structure of the c4-type zinc finger domain from human peroxisome proliferator-activated receptor delta
Structure deposition date
2007-03-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
65
Minimum pKa ?
5
% buried
54
Peptide accession
Q03181
Residue number A
74
Residue number B
133
Peptide name
Peroxisome proliferator-activated receptor delta

Ligandability

Cysteine 74 of Peroxisome proliferator-activated receptor delta

Cysteine 133 of Peroxisome proliferator-activated receptor delta

A redox-regulated disulphide may form within Peroxisome proliferator-activated receptor delta between cysteines 94 and 133. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
2env
Structure name
solution structure of the c4-type zinc finger domain from human peroxisome proliferator-activated receptor delta
Structure deposition date
2007-03-28
Thiol separation (Å)
6
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
62
Peptide accession
Q03181
Residue number A
94
Residue number B
133
Peptide name
Peroxisome proliferator-activated receptor delta

Ligandability

Cysteine 94 of Peroxisome proliferator-activated receptor delta

Cysteine 133 of Peroxisome proliferator-activated receptor delta

A redox-regulated disulphide may form within Peroxisome proliferator-activated receptor delta between cysteines 91 and 133. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
2env
Structure name
solution structure of the c4-type zinc finger domain from human peroxisome proliferator-activated receptor delta
Structure deposition date
2007-03-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
8
% buried
48
Peptide accession
Q03181
Residue number A
91
Residue number B
133
Peptide name
Peroxisome proliferator-activated receptor delta

Ligandability

Cysteine 91 of Peroxisome proliferator-activated receptor delta

Cysteine 133 of Peroxisome proliferator-activated receptor delta

A redox-regulated disulphide may form within Peroxisome proliferator-activated receptor delta between cysteines 77 and 133. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
2env
Structure name
solution structure of the c4-type zinc finger domain from human peroxisome proliferator-activated receptor delta
Structure deposition date
2007-03-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
50
Peptide accession
Q03181
Residue number A
77
Residue number B
133
Peptide name
Peroxisome proliferator-activated receptor delta

Ligandability

Cysteine 77 of Peroxisome proliferator-activated receptor delta

Cysteine 133 of Peroxisome proliferator-activated receptor delta

A redox-regulated disulphide may form within Peroxisome proliferator-activated receptor delta between cysteines 249 and 251. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
5u3z
Structure name
human ppardelta ligand-binding domain in complexed with specific agonist 10
Structure deposition date
2016-12-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
11
% buried
83
Peptide accession
Q03181
Residue number A
249
Residue number B
251
Peptide name
Peroxisome proliferator-activated receptor delta

Ligandability

Cysteine 249 of Peroxisome proliferator-activated receptor delta

Cysteine 251 of Peroxisome proliferator-activated receptor delta

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