ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Interleukin-13 receptor subunit alpha-1

Intermolecular
Cysteine 151 of Interleukin-4 and cysteine 257
Cysteine 151 of Interleukin-4 and cysteine 320
Intramolecular
Cysteine 62 and cysteine 102
Cysteine 173 and cysteine 185
Cysteine 282 and cysteine 296
Cysteine 134 and cysteine 144
Cysteine 95 and cysteine 117
Cysteine 257 and cysteine 320
Cysteine 144 and cysteine 173
Cysteine 144 and cysteine 185
More...
Cysteine 134 and cysteine 173
Cysteine 134 and cysteine 185
A redox-regulated disulphide may form between cysteine 151 of Interleukin-4 and cysteine 257 of Interleukin-13 receptor subunit alpha-1 (127 and 257 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
3bpn
Structure name
crystal structure of the il4-il4r-il13ra ternary complex
Structure deposition date
2007-12-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide A name
Interleukin-4
Peptide B name
Interleukin-13 receptor subunit alpha-1
Peptide A accession
P05112
Peptide B accession
P78552
Peptide A residue number
151
Peptide B residue number
257

Ligandability

Cysteine 151 of Interleukin-4

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 257 of Interleukin-13 receptor subunit alpha-1

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 between cysteine 151 of Interleukin-4 and cysteine 320 of Interleukin-13 receptor subunit alpha-1 (127 and 320 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
3bpn
Structure name
crystal structure of the il4-il4r-il13ra ternary complex
Structure deposition date
2007-12-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide A name
Interleukin-4
Peptide B name
Interleukin-13 receptor subunit alpha-1
Peptide A accession
P05112
Peptide B accession
P78552
Peptide A residue number
151
Peptide B residue number
320

Ligandability

Cysteine 151 of Interleukin-4

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 320 of Interleukin-13 receptor subunit alpha-1

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-1 between cysteines 62 and 102.

Details

Redox score ?
87
PDB code
5e4e
Structure name
engineered interleukin-13 bound to receptor
Structure deposition date
2015-10-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78552
Residue number A
62
Residue number B
102
Peptide name
Interleukin-13 receptor subunit alpha-1

Ligandability

Cysteine 62 of Interleukin-13 receptor subunit alpha-1

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 102 of Interleukin-13 receptor subunit alpha-1

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-1 between cysteines 173 and 185.

Details

Redox score ?
85
PDB code
5e4e
Structure name
engineered interleukin-13 bound to receptor
Structure deposition date
2015-10-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78552
Residue number A
173
Residue number B
185
Peptide name
Interleukin-13 receptor subunit alpha-1

Ligandability

Cysteine 173 of Interleukin-13 receptor subunit alpha-1

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 185 of Interleukin-13 receptor subunit alpha-1

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-1 between cysteines 282 and 296.

Details

Redox score ?
84
PDB code
3bpo
Structure name
crystal structure of the il13-il4r-il13ra ternary complex
Structure deposition date
2007-12-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78552
Residue number A
282
Residue number B
296
Peptide name
Interleukin-13 receptor subunit alpha-1

Ligandability

Cysteine 282 of Interleukin-13 receptor subunit alpha-1

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 296 of Interleukin-13 receptor subunit alpha-1

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-1 between cysteines 134 and 144.

Details

Redox score ?
84
PDB code
3bpo
Structure name
crystal structure of the il13-il4r-il13ra ternary complex
Structure deposition date
2007-12-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78552
Residue number A
134
Residue number B
144
Peptide name
Interleukin-13 receptor subunit alpha-1

Ligandability

Cysteine 134 of Interleukin-13 receptor subunit alpha-1

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 144 of Interleukin-13 receptor subunit alpha-1

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-1 between cysteines 95 and 117.

Details

Redox score ?
83
PDB code
5e4e
Structure name
engineered interleukin-13 bound to receptor
Structure deposition date
2015-10-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78552
Residue number A
95
Residue number B
117
Peptide name
Interleukin-13 receptor subunit alpha-1

Ligandability

Cysteine 95 of Interleukin-13 receptor subunit alpha-1

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 117 of Interleukin-13 receptor subunit alpha-1

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-1 between cysteines 257 and 320.

Details

Redox score ?
82
PDB code
3bpo
Structure name
crystal structure of the il13-il4r-il13ra ternary complex
Structure deposition date
2007-12-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78552
Residue number A
257
Residue number B
320
Peptide name
Interleukin-13 receptor subunit alpha-1

Ligandability

Cysteine 257 of Interleukin-13 receptor subunit alpha-1

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 320 of Interleukin-13 receptor subunit alpha-1

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-1 between cysteines 144 and 173. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
3bpn
Structure name
crystal structure of the il4-il4r-il13ra ternary complex
Structure deposition date
2007-12-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78552
Residue number A
144
Residue number B
173
Peptide name
Interleukin-13 receptor subunit alpha-1

Ligandability

Cysteine 144 of Interleukin-13 receptor subunit alpha-1

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 173 of Interleukin-13 receptor subunit alpha-1

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-1 between cysteines 144 and 185. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
3bpo
Structure name
crystal structure of the il13-il4r-il13ra ternary complex
Structure deposition date
2007-12-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78552
Residue number A
144
Residue number B
185
Peptide name
Interleukin-13 receptor subunit alpha-1

Ligandability

Cysteine 144 of Interleukin-13 receptor subunit alpha-1

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 185 of Interleukin-13 receptor subunit alpha-1

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-1 between cysteines 134 and 173. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
5e4e
Structure name
engineered interleukin-13 bound to receptor
Structure deposition date
2015-10-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78552
Residue number A
134
Residue number B
173
Peptide name
Interleukin-13 receptor subunit alpha-1

Ligandability

Cysteine 134 of Interleukin-13 receptor subunit alpha-1

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 173 of Interleukin-13 receptor subunit alpha-1

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-1 between cysteines 134 and 185. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
5e4e
Structure name
engineered interleukin-13 bound to receptor
Structure deposition date
2015-10-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78552
Residue number A
134
Residue number B
185
Peptide name
Interleukin-13 receptor subunit alpha-1

Ligandability

Cysteine 134 of Interleukin-13 receptor subunit alpha-1

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 185 of Interleukin-13 receptor subunit alpha-1

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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