ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Interleukin-21 receptor

Intramolecular
Cysteine 20 and cysteine 109
Cysteine 25 and cysteine 35
Cysteine 65 and cysteine 81
Cysteine 35 and cysteine 81
Cysteine 20 and cysteine 25
Cysteine 25 and cysteine 109
Cysteine 35 and cysteine 109
Cysteine 25 and cysteine 81
Cysteine 35 and cysteine 65
Cysteine 25 and cysteine 65
A redox-regulated disulphide may form within Interleukin-21 receptor between cysteines 20 and 109 (1 and 90 respectively in this structure).

Details

Redox score ?
89
PDB code
3tgx
Structure name
il-21:il21r complex
Structure deposition date
2011-08-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9HBE5
Residue number A
20
Residue number B
109
Peptide name
Interleukin-21 receptor

Ligandability

Cysteine 20 of Interleukin-21 receptor

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 109 of Interleukin-21 receptor

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-21 receptor between cysteines 25 and 35 (6 and 16 respectively in this structure).

Details

Redox score ?
83
PDB code
3tgx
Structure name
il-21:il21r complex
Structure deposition date
2011-08-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9HBE5
Residue number A
25
Residue number B
35
Peptide name
Interleukin-21 receptor

Ligandability

Cysteine 25 of Interleukin-21 receptor

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 35 of Interleukin-21 receptor

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-21 receptor between cysteines 65 and 81 (46 and 62 respectively in this structure).

Details

Redox score ?
79
PDB code
3tgx
Structure name
il-21:il21r complex
Structure deposition date
2011-08-18
Thiol separation (Å)
3
Half-sphere exposure sum ?
57
Minimum pKa ?
8
% buried
44
Peptide accession
Q9HBE5
Residue number A
65
Residue number B
81
Peptide name
Interleukin-21 receptor

Ligandability

Cysteine 65 of Interleukin-21 receptor

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 81 of Interleukin-21 receptor

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-21 receptor between cysteines 35 and 81 (16 and 62 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
4nzd
Structure name
interleukin 21 receptor
Structure deposition date
2013-12-12
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9HBE5
Residue number A
35
Residue number B
81
Peptide name
Interleukin-21 receptor

Ligandability

Cysteine 35 of Interleukin-21 receptor

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 81 of Interleukin-21 receptor

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-21 receptor between cysteines 20 and 25 (1 and 6 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
4nzd
Structure name
interleukin 21 receptor
Structure deposition date
2013-12-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9HBE5
Residue number A
20
Residue number B
25
Peptide name
Interleukin-21 receptor

Ligandability

Cysteine 20 of Interleukin-21 receptor

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 25 of Interleukin-21 receptor

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-21 receptor between cysteines 25 and 109 (6 and 90 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
4nzd
Structure name
interleukin 21 receptor
Structure deposition date
2013-12-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9HBE5
Residue number A
25
Residue number B
109
Peptide name
Interleukin-21 receptor

Ligandability

Cysteine 25 of Interleukin-21 receptor

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 109 of Interleukin-21 receptor

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-21 receptor between cysteines 35 and 109 (16 and 90 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
4nzd
Structure name
interleukin 21 receptor
Structure deposition date
2013-12-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9HBE5
Residue number A
35
Residue number B
109
Peptide name
Interleukin-21 receptor

Ligandability

Cysteine 35 of Interleukin-21 receptor

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 109 of Interleukin-21 receptor

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-21 receptor between cysteines 25 and 81 (6 and 62 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
3tgx
Structure name
il-21:il21r complex
Structure deposition date
2011-08-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
12
% buried
nan
Peptide accession
Q9HBE5
Residue number A
25
Residue number B
81
Peptide name
Interleukin-21 receptor

Ligandability

Cysteine 25 of Interleukin-21 receptor

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 81 of Interleukin-21 receptor

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-21 receptor between cysteines 35 and 65 (16 and 46 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
3tgx
Structure name
il-21:il21r complex
Structure deposition date
2011-08-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
17
% buried
nan
Peptide accession
Q9HBE5
Residue number A
35
Residue number B
65
Peptide name
Interleukin-21 receptor

Ligandability

Cysteine 35 of Interleukin-21 receptor

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 65 of Interleukin-21 receptor

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-21 receptor between cysteines 25 and 65 (6 and 46 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
3tgx
Structure name
il-21:il21r complex
Structure deposition date
2011-08-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
16
% buried
nan
Peptide accession
Q9HBE5
Residue number A
25
Residue number B
65
Peptide name
Interleukin-21 receptor

Ligandability

Cysteine 25 of Interleukin-21 receptor

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 65 of Interleukin-21 receptor

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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