ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Interleukin-2 receptor subunit beta

Intramolecular
Cysteine 194 and cysteine 312
Cysteine 31 and cysteine 123
Cysteine 36 and cysteine 46
Cysteine 59 and cysteine 110
Cysteine 74 and cysteine 86
Cysteine 46 and cysteine 86
Cysteine 46 and cysteine 74
Cysteine 36 and cysteine 86
Cysteine 36 and cysteine 74
Cysteine 59 and cysteine 86
More...
Cysteine 148 and cysteine 194
Cysteine 148 and cysteine 312
A redox-regulated disulphide may form within Interleukin-2 receptor subunit beta between cysteines 194 and 312 (168 and 312 respectively in this structure).

Details

Redox score ?
87
PDB code
5m5e
Structure name
crystal structure of a interleukin-2 variant in complex with interleukin-2 receptor
Structure deposition date
2016-10-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14784
Residue number A
194
Residue number B
312
Peptide name
Interleukin-2 receptor subunit beta

Ligandability

Cysteine 194 of Interleukin-2 receptor subunit beta

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 312 of Interleukin-2 receptor subunit beta

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 312 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Interleukin-2 receptor subunit beta between cysteines 31 and 123.

Details

Redox score ?
86
PDB code
6dg5
Structure name
structure of a de novo designed interleukin-2/interleukin-15 mimetic complex with il-2rb and il-2rg
Structure deposition date
2018-05-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16297
Residue number A
31
Residue number B
123
Peptide name
Interleukin-2 receptor subunit beta

Ligandability

Cysteine 31 of Interleukin-2 receptor subunit beta

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 123 of Interleukin-2 receptor subunit beta

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-2 receptor subunit beta between cysteines 36 and 46 (10 and 20 respectively in this structure).

Details

Redox score ?
84
PDB code
3qaz
Structure name
il-2 mutant d10 ternary complex
Structure deposition date
2011-01-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14784
Residue number A
36
Residue number B
46
Peptide name
Interleukin-2 receptor subunit beta

Ligandability

Cysteine 36 of Interleukin-2 receptor subunit beta

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 46 of Interleukin-2 receptor subunit beta

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-2 receptor subunit beta between cysteines 59 and 110 (33 and 84 respectively in this structure).

Details

Redox score ?
83
PDB code
3qaz
Structure name
il-2 mutant d10 ternary complex
Structure deposition date
2011-01-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14784
Residue number A
59
Residue number B
110
Peptide name
Interleukin-2 receptor subunit beta

Ligandability

Cysteine 59 of Interleukin-2 receptor subunit beta

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 110 of Interleukin-2 receptor subunit beta

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-2 receptor subunit beta between cysteines 74 and 86 (48 and 60 respectively in this structure).

Details

Redox score ?
82
PDB code
4gs7
Structure name
structure of the interleukin-15 quaternary complex
Structure deposition date
2012-08-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14784
Residue number A
74
Residue number B
86
Peptide name
Interleukin-2 receptor subunit beta

Ligandability

Cysteine 74 of Interleukin-2 receptor subunit beta

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 86 of Interleukin-2 receptor subunit beta

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-2 receptor subunit beta between cysteines 46 and 86 (20 and 60 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
3qaz
Structure name
il-2 mutant d10 ternary complex
Structure deposition date
2011-01-12
Thiol separation (Å)
6
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14784
Residue number A
46
Residue number B
86
Peptide name
Interleukin-2 receptor subunit beta

Ligandability

Cysteine 46 of Interleukin-2 receptor subunit beta

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 86 of Interleukin-2 receptor subunit beta

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-2 receptor subunit beta between cysteines 46 and 74 (20 and 48 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
3qaz
Structure name
il-2 mutant d10 ternary complex
Structure deposition date
2011-01-12
Thiol separation (Å)
7
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14784
Residue number A
46
Residue number B
74
Peptide name
Interleukin-2 receptor subunit beta

Ligandability

Cysteine 46 of Interleukin-2 receptor subunit beta

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 74 of Interleukin-2 receptor subunit beta

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-2 receptor subunit beta between cysteines 36 and 86 (10 and 60 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
3qaz
Structure name
il-2 mutant d10 ternary complex
Structure deposition date
2011-01-12
Thiol separation (Å)
8
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14784
Residue number A
36
Residue number B
86
Peptide name
Interleukin-2 receptor subunit beta

Ligandability

Cysteine 36 of Interleukin-2 receptor subunit beta

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 86 of Interleukin-2 receptor subunit beta

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-2 receptor subunit beta between cysteines 36 and 74 (10 and 48 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
3qaz
Structure name
il-2 mutant d10 ternary complex
Structure deposition date
2011-01-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14784
Residue number A
36
Residue number B
74
Peptide name
Interleukin-2 receptor subunit beta

Ligandability

Cysteine 36 of Interleukin-2 receptor subunit beta

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 74 of Interleukin-2 receptor subunit beta

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-2 receptor subunit beta between cysteines 59 and 86 (33 and 60 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
3qaz
Structure name
il-2 mutant d10 ternary complex
Structure deposition date
2011-01-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14784
Residue number A
59
Residue number B
86
Peptide name
Interleukin-2 receptor subunit beta

Ligandability

Cysteine 59 of Interleukin-2 receptor subunit beta

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 86 of Interleukin-2 receptor subunit beta

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-2 receptor subunit beta between cysteines 148 and 194 (122 and 168 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
3qaz
Structure name
il-2 mutant d10 ternary complex
Structure deposition date
2011-01-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
12
% buried
94
Peptide accession
P14784
Residue number A
148
Residue number B
194
Peptide name
Interleukin-2 receptor subunit beta

Ligandability

Cysteine 148 of Interleukin-2 receptor subunit beta

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 194 of Interleukin-2 receptor subunit beta

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-2 receptor subunit beta between cysteines 148 and 312 (122 and 312 respectively in this structure).

Details

Redox score ?
nan
PDB code
5m5e
Structure name
crystal structure of a interleukin-2 variant in complex with interleukin-2 receptor
Structure deposition date
2016-10-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
nan
Minimum pKa ?
12
% buried
nan
Peptide accession
P14784
Residue number A
148
Residue number B
312
Peptide name
Interleukin-2 receptor subunit beta

Ligandability

Cysteine 148 of Interleukin-2 receptor subunit beta

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 312 of Interleukin-2 receptor subunit beta

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 312 in protein B could not be asigned to a Uniprot residue.
If this tool was useful for finding a disulphide, please cite: