ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Interferon-induced, double-stranded RNA-activated protein kinase

Intramolecular
Cysteine 116 and cysteine 128
Cysteine 128 and cysteine 130
A redox-regulated disulphide may form within Interferon-induced, double-stranded RNA-activated protein kinase between cysteines 116 and 128 (28 and 40 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
1x48
Structure name
solution structure of the second dsrm domain in interferon-induced, double-stranded rna-activated protein kinase
Structure deposition date
2005-05-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
8
Peptide accession
Q03963
Residue number A
116
Residue number B
128
Peptide name
Interferon-induced, double-stranded RNA-activated protein kinase

Ligandability

Cysteine 116 of Interferon-induced, double-stranded RNA-activated protein kinase

Cysteine 128 of Interferon-induced, double-stranded RNA-activated protein kinase

A redox-regulated disulphide may form within Interferon-induced, double-stranded RNA-activated protein kinase between cysteines 128 and 130 (40 and 42 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
1x48
Structure name
solution structure of the second dsrm domain in interferon-induced, double-stranded rna-activated protein kinase
Structure deposition date
2005-05-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
32
Peptide accession
Q03963
Residue number A
128
Residue number B
130
Peptide name
Interferon-induced, double-stranded RNA-activated protein kinase

Ligandability

Cysteine 128 of Interferon-induced, double-stranded RNA-activated protein kinase

Cysteine 130 of Interferon-induced, double-stranded RNA-activated protein kinase

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