ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Interferon regulatory factor 3

Intramolecular
Cysteine 267 and cysteine 289
Cysteine 289 and cysteine 347
Cysteine 347 and cysteine 120 L
A redox-regulated disulphide may form within Interferon regulatory factor 3 between cysteines 267 and 289.

Details

Redox score ?
68
PDB code
7jfl
Structure name
crystal structure of human phosphorylated irf-3 bound to cbp
Structure deposition date
2020-07-17
Thiol separation (Å)
5
Half-sphere exposure sum ?
66
Minimum pKa ?
9
% buried
36
Peptide accession
Q14653
Residue number A
267
Residue number B
289
Peptide name
Interferon regulatory factor 3

Ligandability

Cysteine 267 of Interferon regulatory factor 3

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 289 of Interferon regulatory factor 3

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 Interferon regulatory factor 3 between cysteines 289 and 347. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
5jer
Structure name
structure of rotavirus nsp1 bound to irf-3
Structure deposition date
2016-04-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
92
Peptide accession
Q14653
Residue number A
289
Residue number B
347
Peptide name
Interferon regulatory factor 3

Ligandability

Cysteine 289 of Interferon regulatory factor 3

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 347 of Interferon regulatory factor 3

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 Interferon regulatory factor 3 between cysteines 347 and 120 (38 and 120 respectively in this structure).

Details

Redox score ?
nan
PDB code
2o61
Structure name
crystal structure of nfkb, irf7, irf3 bound to the interferon-b enhancer
Structure deposition date
2006-12-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
48
Minimum pKa ?
12
% buried
80
Peptide accession
Q14653
Residue number A
347
Residue number B
120
Peptide name
Interferon regulatory factor 3

Ligandability

Cysteine 347 of Interferon regulatory factor 3

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 120 of Interferon regulatory factor 3

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.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Uncertain whether structure cysteine 38 has been assigned to correct residue.
Cysteine 120 in protein B could not be asigned to a Uniprot residue.
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