ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Interleukin-10

Intermolecular
Cysteine 132 and cysteine 132
Cysteine 80 and cysteine 132
Intramolecular
Cysteine 30 and cysteine 126
Cysteine 80 and cysteine 132
A redox-regulated disulphide may form between two units of Interleukin-10 at cysteines 132 and 132 (114 and 114 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
4x51
Structure name
x-ray structure of mouse interleukin-10 mutant - s1_e8del, c149y
Structure deposition date
2014-12-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide A name
Interleukin-10
Peptide B name
Interleukin-10
Peptide A accession
P18893
Peptide B accession
P18893
Peptide A residue number
132
Peptide B residue number
132

Ligandability

A redox-regulated disulphide may form between two units of Interleukin-10 at cysteines 80 and 132 (62 and 114 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
4x51
Structure name
x-ray structure of mouse interleukin-10 mutant - s1_e8del, c149y
Structure deposition date
2014-12-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide A name
Interleukin-10
Peptide B name
Interleukin-10
Peptide A accession
P18893
Peptide B accession
P18893
Peptide A residue number
80
Peptide B residue number
132

Ligandability

Cysteine 80 of Interleukin-10

Cysteine 132 of Interleukin-10

A redox-regulated disulphide may form within Interleukin-10 between cysteines 30 and 126 (12 and 108 respectively in this structure).

Details

Redox score ?
88
PDB code
1j7v
Structure name
human il-10 / il-10r1 complex
Structure deposition date
2001-05-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
41
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22301
Residue number A
30
Residue number B
126
Peptide name
Interleukin-10

Ligandability

Cysteine 30 of Interleukin-10

Cysteine 126 of Interleukin-10

A redox-regulated disulphide may form within Interleukin-10 between cysteines 80 and 132 (62 and 114 respectively in this structure).

Details

Redox score ?
83
PDB code
2h24
Structure name
crystal structure of human il-10
Structure deposition date
2006-05-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22301
Residue number A
80
Residue number B
132
Peptide name
Interleukin-10

Ligandability

Cysteine 80 of Interleukin-10

Cysteine 132 of Interleukin-10

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