ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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NF-kappa-B inhibitor alpha

Intramolecular
Cysteine 152 and cysteine 186
Cysteine 135 and cysteine 167
Cysteine 152 and cysteine 156
A redox-regulated disulphide may form within NF-kappa-B inhibitor alpha between cysteines 152 and 186.

Details

Redox score ?
73
PDB code
1nfi
Structure name
i-kappa-b-alpha/nf-kappa-b complex
Structure deposition date
1998-08-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
92
Minimum pKa ?
5
% buried
100
Peptide accession
P25963
Residue number A
152
Residue number B
186
Peptide name
NF-kappa-B inhibitor alpha

Ligandability

Cysteine 152 of NF-kappa-B inhibitor alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 186 of NF-kappa-B inhibitor alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within NF-kappa-B inhibitor alpha between cysteines 135 and 167. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
1nfi
Structure name
i-kappa-b-alpha/nf-kappa-b complex
Structure deposition date
1998-08-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
65
Peptide accession
P25963
Residue number A
135
Residue number B
167
Peptide name
NF-kappa-B inhibitor alpha

Ligandability

Cysteine 135 of NF-kappa-B inhibitor alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 167 of NF-kappa-B inhibitor alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within NF-kappa-B inhibitor alpha between cysteines 152 and 156. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
1ikn
Structure name
ikappabalpha/nf-kappab complex
Structure deposition date
1998-11-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
8
% buried
62
Peptide accession
P25963
Residue number A
152
Residue number B
156
Peptide name
NF-kappa-B inhibitor alpha

Ligandability

Cysteine 152 of NF-kappa-B inhibitor alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 156 of NF-kappa-B inhibitor alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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