ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Interleukin-20

Intramolecular
Cysteine 80 and cysteine 132
Cysteine 33 and cysteine 126
Cysteine 81 and cysteine 134
Cysteine 33 and cysteine 80
Cysteine 80 and cysteine 126
Cysteine 33 and cysteine 132
Cysteine 126 and cysteine 132
Cysteine 132 and cysteine 134
Cysteine 81 and cysteine 132
Cysteine 80 and cysteine 134
Cysteine 80 and cysteine 81
A redox-regulated disulphide may form within Interleukin-20 between cysteines 80 and 132.

Details

Redox score ?
82
PDB code
4doh
Structure name
il20/il201/il20r2 ternary complex
Structure deposition date
2012-02-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NYY1
Residue number A
80
Residue number B
132
Peptide name
Interleukin-20

Ligandability

Cysteine 80 of Interleukin-20

Cysteine 132 of Interleukin-20

A redox-regulated disulphide may form within Interleukin-20 between cysteines 33 and 126.

Details

Redox score ?
82
PDB code
4doh
Structure name
il20/il201/il20r2 ternary complex
Structure deposition date
2012-02-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NYY1
Residue number A
33
Residue number B
126
Peptide name
Interleukin-20

Ligandability

Cysteine 33 of Interleukin-20

Cysteine 126 of Interleukin-20

A redox-regulated disulphide may form within Interleukin-20 between cysteines 81 and 134.

Details

Redox score ?
80
PDB code
4doh
Structure name
il20/il201/il20r2 ternary complex
Structure deposition date
2012-02-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NYY1
Residue number A
81
Residue number B
134
Peptide name
Interleukin-20

Ligandability

Cysteine 81 of Interleukin-20

Cysteine 134 of Interleukin-20

A redox-regulated disulphide may form within Interleukin-20 between cysteines 33 and 80.

Details

Redox score ?
71
PDB code
4doh
Structure name
il20/il201/il20r2 ternary complex
Structure deposition date
2012-02-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NYY1
Residue number A
33
Residue number B
80
Peptide name
Interleukin-20

Ligandability

Cysteine 33 of Interleukin-20

Cysteine 80 of Interleukin-20

A redox-regulated disulphide may form within Interleukin-20 between cysteines 80 and 126.

Details

Redox score ?
64
PDB code
4doh
Structure name
il20/il201/il20r2 ternary complex
Structure deposition date
2012-02-09
Thiol separation (Å)
5
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NYY1
Residue number A
80
Residue number B
126
Peptide name
Interleukin-20

Ligandability

Cysteine 80 of Interleukin-20

Cysteine 126 of Interleukin-20

A redox-regulated disulphide may form within Interleukin-20 between cysteines 33 and 132.

Details

Redox score ?
63
PDB code
4doh
Structure name
il20/il201/il20r2 ternary complex
Structure deposition date
2012-02-09
Thiol separation (Å)
6
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NYY1
Residue number A
33
Residue number B
132
Peptide name
Interleukin-20

Ligandability

Cysteine 33 of Interleukin-20

Cysteine 132 of Interleukin-20

A redox-regulated disulphide may form within Interleukin-20 between cysteines 126 and 132.

Details

Redox score ?
61
PDB code
4doh
Structure name
il20/il201/il20r2 ternary complex
Structure deposition date
2012-02-09
Thiol separation (Å)
6
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NYY1
Residue number A
126
Residue number B
132
Peptide name
Interleukin-20

Ligandability

Cysteine 126 of Interleukin-20

Cysteine 132 of Interleukin-20

A redox-regulated disulphide may form within Interleukin-20 between cysteines 132 and 134.

Details

Redox score ?
60
PDB code
4doh
Structure name
il20/il201/il20r2 ternary complex
Structure deposition date
2012-02-09
Thiol separation (Å)
6
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NYY1
Residue number A
132
Residue number B
134
Peptide name
Interleukin-20

Ligandability

Cysteine 132 of Interleukin-20

Cysteine 134 of Interleukin-20

A redox-regulated disulphide may form within Interleukin-20 between cysteines 81 and 132. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
4doh
Structure name
il20/il201/il20r2 ternary complex
Structure deposition date
2012-02-09
Thiol separation (Å)
6
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NYY1
Residue number A
81
Residue number B
132
Peptide name
Interleukin-20

Ligandability

Cysteine 81 of Interleukin-20

Cysteine 132 of Interleukin-20

A redox-regulated disulphide may form within Interleukin-20 between cysteines 80 and 134. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
4doh
Structure name
il20/il201/il20r2 ternary complex
Structure deposition date
2012-02-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NYY1
Residue number A
80
Residue number B
134
Peptide name
Interleukin-20

Ligandability

Cysteine 80 of Interleukin-20

Cysteine 134 of Interleukin-20

A redox-regulated disulphide may form within Interleukin-20 between cysteines 80 and 81. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
4doh
Structure name
il20/il201/il20r2 ternary complex
Structure deposition date
2012-02-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NYY1
Residue number A
80
Residue number B
81
Peptide name
Interleukin-20

Ligandability

Cysteine 80 of Interleukin-20

Cysteine 81 of Interleukin-20

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