ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Interferon alpha/beta receptor 2

Intermolecular
Cysteine 227 and cysteine 227
Cysteine 227 and cysteine 207
Intramolecular
Cysteine 85 and cysteine 93
Cysteine 39 and cysteine 122
Cysteine 207 and cysteine 227
A redox-regulated disulphide may form between two units of Interferon alpha/beta receptor 2 at cysteines 227 and 227 (200 and 200 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
3s8w
Structure name
d2 domain of human ifnar2
Structure deposition date
2011-05-31
Thiol separation (Å)
7
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide A name
Interferon alpha/beta receptor 2
Peptide B name
Interferon alpha/beta receptor 2
Peptide A accession
P48551
Peptide B accession
P48551
Peptide A residue number
227
Peptide B residue number
227

Ligandability

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 two units of Interferon alpha/beta receptor 2 at cysteines 227 and 207 (200 and 180 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
3s8w
Structure name
d2 domain of human ifnar2
Structure deposition date
2011-05-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide A name
Interferon alpha/beta receptor 2
Peptide B name
Interferon alpha/beta receptor 2
Peptide A accession
P48551
Peptide B accession
P48551
Peptide A residue number
227
Peptide B residue number
207

Ligandability

Cysteine 227 of Interferon alpha/beta receptor 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 207 of Interferon alpha/beta receptor 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 Interferon alpha/beta receptor 2 between cysteines 85 and 93 (58 and 66 respectively in this structure).

Details

Redox score ?
85
PDB code
3se4
Structure name
human ifnw-ifnar ternary complex
Structure deposition date
2011-06-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P48551
Residue number A
85
Residue number B
93
Peptide name
Interferon alpha/beta receptor 2

Ligandability

Cysteine 85 of Interferon alpha/beta receptor 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 93 of Interferon alpha/beta receptor 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 Interferon alpha/beta receptor 2 between cysteines 39 and 122 (12 and 95 respectively in this structure).

Details

Redox score ?
84
PDB code
2hym
Structure name
nmr based docking model of the complex between the human type i interferon receptor and human interferon alpha-2
Structure deposition date
2006-08-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15467
Residue number A
39
Residue number B
122
Peptide name
Interferon alpha/beta receptor 2

Ligandability

Cysteine 39 of Interferon alpha/beta receptor 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 122 of Interferon alpha/beta receptor 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 Interferon alpha/beta receptor 2 between cysteines 207 and 227 (180 and 200 respectively in this structure).

Details

Redox score ?
79
PDB code
2hym
Structure name
nmr based docking model of the complex between the human type i interferon receptor and human interferon alpha-2
Structure deposition date
2006-08-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15467
Residue number A
207
Residue number B
227
Peptide name
Interferon alpha/beta receptor 2

Ligandability

Cysteine 207 of Interferon alpha/beta receptor 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 227 of Interferon alpha/beta receptor 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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