ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Interleukin-13 receptor subunit alpha-2

Intramolecular
Cysteine 65 and cysteine 113
Cysteine 184 and cysteine 197
Cysteine 305 and cysteine 330
Cysteine 145 and cysteine 155
Cysteine 269 and cysteine 316
Cysteine 155 and cysteine 197
Cysteine 155 and cysteine 184
Cysteine 145 and cysteine 197
A redox-regulated disulphide may form within Interleukin-13 receptor subunit alpha-2 between cysteines 65 and 113.

Details

Redox score ?
88
PDB code
3lb6
Structure name
the structure of il-13 in complex with il-13ralpha2
Structure deposition date
2010-01-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
33
Minimum pKa ?
nan
% buried
nan
Peptide accession
A8K7E2
Residue number A
65
Residue number B
113
Peptide name
Interleukin-13 receptor subunit alpha-2

Ligandability

Cysteine 65 of Interleukin-13 receptor subunit alpha-2

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 113 of Interleukin-13 receptor subunit alpha-2

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 Interleukin-13 receptor subunit alpha-2 between cysteines 184 and 197.

Details

Redox score ?
87
PDB code
3lb6
Structure name
the structure of il-13 in complex with il-13ralpha2
Structure deposition date
2010-01-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
A8K7E2
Residue number A
184
Residue number B
197
Peptide name
Interleukin-13 receptor subunit alpha-2

Ligandability

Cysteine 184 of Interleukin-13 receptor subunit alpha-2

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 197 of Interleukin-13 receptor subunit alpha-2

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 Interleukin-13 receptor subunit alpha-2 between cysteines 305 and 330.

Details

Redox score ?
84
PDB code
3lb6
Structure name
the structure of il-13 in complex with il-13ralpha2
Structure deposition date
2010-01-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
A8K7E2
Residue number A
305
Residue number B
330
Peptide name
Interleukin-13 receptor subunit alpha-2

Ligandability

Cysteine 305 of Interleukin-13 receptor subunit alpha-2

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 330 of Interleukin-13 receptor subunit alpha-2

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 Interleukin-13 receptor subunit alpha-2 between cysteines 145 and 155.

Details

Redox score ?
84
PDB code
3lb6
Structure name
the structure of il-13 in complex with il-13ralpha2
Structure deposition date
2010-01-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
A8K7E2
Residue number A
145
Residue number B
155
Peptide name
Interleukin-13 receptor subunit alpha-2

Ligandability

Cysteine 145 of Interleukin-13 receptor subunit alpha-2

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 155 of Interleukin-13 receptor subunit alpha-2

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 Interleukin-13 receptor subunit alpha-2 between cysteines 269 and 316.

Details

Redox score ?
82
PDB code
3lb6
Structure name
the structure of il-13 in complex with il-13ralpha2
Structure deposition date
2010-01-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
A8K7E2
Residue number A
269
Residue number B
316
Peptide name
Interleukin-13 receptor subunit alpha-2

Ligandability

Cysteine 269 of Interleukin-13 receptor subunit alpha-2

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 316 of Interleukin-13 receptor subunit alpha-2

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 Interleukin-13 receptor subunit alpha-2 between cysteines 155 and 197. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
3lb6
Structure name
the structure of il-13 in complex with il-13ralpha2
Structure deposition date
2010-01-07
Thiol separation (Å)
6
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
A8K7E2
Residue number A
155
Residue number B
197
Peptide name
Interleukin-13 receptor subunit alpha-2

Ligandability

Cysteine 155 of Interleukin-13 receptor subunit alpha-2

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 197 of Interleukin-13 receptor subunit alpha-2

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 Interleukin-13 receptor subunit alpha-2 between cysteines 155 and 184. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
3lb6
Structure name
the structure of il-13 in complex with il-13ralpha2
Structure deposition date
2010-01-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
A8K7E2
Residue number A
155
Residue number B
184
Peptide name
Interleukin-13 receptor subunit alpha-2

Ligandability

Cysteine 155 of Interleukin-13 receptor subunit alpha-2

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 184 of Interleukin-13 receptor subunit alpha-2

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 Interleukin-13 receptor subunit alpha-2 between cysteines 145 and 197. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
3lb6
Structure name
the structure of il-13 in complex with il-13ralpha2
Structure deposition date
2010-01-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
A8K7E2
Residue number A
145
Residue number B
197
Peptide name
Interleukin-13 receptor subunit alpha-2

Ligandability

Cysteine 145 of Interleukin-13 receptor subunit alpha-2

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 197 of Interleukin-13 receptor subunit alpha-2

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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