ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Interleukin-1 receptor type 1

Intramolecular
Cysteine 23 and cysteine 104
Cysteine 121 and cysteine 164
Cysteine 44 and cysteine 96
Cysteine 248 and cysteine 312
Cysteine 142 and cysteine 196
Cysteine 96 and cysteine 104
A redox-regulated disulphide may form within Interleukin-1 receptor type 1 between cysteines 23 and 104 (3 and 84 respectively in this structure).

Details

Redox score ?
88
PDB code
1ira
Structure name
complex of the interleukin-1 receptor with the interleukin-1 receptor antagonist (il1ra)
Structure deposition date
1998-04-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
41
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14778
Residue number A
23
Residue number B
104
Peptide name
Interleukin-1 receptor type 1

Ligandability

Cysteine 23 of Interleukin-1 receptor type 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 104 of Interleukin-1 receptor type 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-1 receptor type 1 between cysteines 121 and 164 (104 and 147 respectively in this structure).

Details

Redox score ?
84
PDB code
1itb
Structure name
type-1 interleukin-1 receptor complexed with interleukin-1 beta
Structure deposition date
1997-01-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14778
Residue number A
121
Residue number B
164
Peptide name
Interleukin-1 receptor type 1

Ligandability

Cysteine 121 of Interleukin-1 receptor type 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 164 of Interleukin-1 receptor type 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-1 receptor type 1 between cysteines 44 and 96 (27 and 79 respectively in this structure).

Details

Redox score ?
82
PDB code
4dep
Structure name
structure of the il-1b signaling complex
Structure deposition date
2012-01-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14778
Residue number A
44
Residue number B
96
Peptide name
Interleukin-1 receptor type 1

Ligandability

Cysteine 44 of Interleukin-1 receptor type 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 96 of Interleukin-1 receptor type 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-1 receptor type 1 between cysteines 248 and 312 (231 and 295 respectively in this structure).

Details

Redox score ?
82
PDB code
4gaf
Structure name
crystal structure of ebi-005, a chimera of human il-1beta and il-1ra, bound to human interleukin-1 receptor type 1
Structure deposition date
2012-07-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14778
Residue number A
248
Residue number B
312
Peptide name
Interleukin-1 receptor type 1

Ligandability

Cysteine 248 of Interleukin-1 receptor type 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 312 of Interleukin-1 receptor type 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-1 receptor type 1 between cysteines 142 and 196 (125 and 179 respectively in this structure).

Details

Redox score ?
79
PDB code
4dep
Structure name
structure of the il-1b signaling complex
Structure deposition date
2012-01-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14778
Residue number A
142
Residue number B
196
Peptide name
Interleukin-1 receptor type 1

Ligandability

Cysteine 142 of Interleukin-1 receptor type 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 196 of Interleukin-1 receptor type 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-1 receptor type 1 between cysteines 96 and 104 (79 and 87 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
1itb
Structure name
type-1 interleukin-1 receptor complexed with interleukin-1 beta
Structure deposition date
1997-01-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14778
Residue number A
96
Residue number B
104
Peptide name
Interleukin-1 receptor type 1

Ligandability

Cysteine 96 of Interleukin-1 receptor type 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 104 of Interleukin-1 receptor type 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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