ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Fc epsilon receptor II

Intramolecular
Cysteine 174 and cysteine 302
Cysteine 177 and cysteine 188
Cysteine 205 and cysteine 296
Cysteine 273 and cysteine 287
Cysteine 174 and cysteine 177
Cysteine 177 and cysteine 302
Cysteine 174 and cysteine 188
Cysteine 188 and cysteine 302
A redox-regulated disulphide may form within Fc epsilon receptor II between cysteines 174 and 302 (162 and 290 respectively in this structure).

Details

Redox score ?
94
PDB code
6pwr
Structure name
crystal structure of the cow c-type carbohydrate-recognition domain of cd23 in the presence of glcnac-beta1-2-man
Structure deposition date
2019-07-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
E1BIQ4
Residue number A
174
Residue number B
302
Peptide name
Fc epsilon receptor II

Ligandability

Cysteine 174 of Fc epsilon receptor II

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 302 of Fc epsilon receptor II

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 Fc epsilon receptor II between cysteines 177 and 188 (165 and 176 respectively in this structure).

Details

Redox score ?
86
PDB code
6pwr
Structure name
crystal structure of the cow c-type carbohydrate-recognition domain of cd23 in the presence of glcnac-beta1-2-man
Structure deposition date
2019-07-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
E1BIQ4
Residue number A
177
Residue number B
188
Peptide name
Fc epsilon receptor II

Ligandability

Cysteine 177 of Fc epsilon receptor II

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 188 of Fc epsilon receptor II

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 Fc epsilon receptor II between cysteines 205 and 296 (193 and 284 respectively in this structure).

Details

Redox score ?
81
PDB code
6pwr
Structure name
crystal structure of the cow c-type carbohydrate-recognition domain of cd23 in the presence of glcnac-beta1-2-man
Structure deposition date
2019-07-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
E1BIQ4
Residue number A
205
Residue number B
296
Peptide name
Fc epsilon receptor II

Ligandability

Cysteine 205 of Fc epsilon receptor II

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 Fc epsilon receptor II

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 Fc epsilon receptor II between cysteines 273 and 287 (261 and 275 respectively in this structure).

Details

Redox score ?
80
PDB code
6pwr
Structure name
crystal structure of the cow c-type carbohydrate-recognition domain of cd23 in the presence of glcnac-beta1-2-man
Structure deposition date
2019-07-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
E1BIQ4
Residue number A
273
Residue number B
287
Peptide name
Fc epsilon receptor II

Ligandability

Cysteine 273 of Fc epsilon receptor II

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 287 of Fc epsilon receptor II

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 Fc epsilon receptor II between cysteines 174 and 177 (162 and 165 respectively in this structure).

Details

Redox score ?
61
PDB code
6pwr
Structure name
crystal structure of the cow c-type carbohydrate-recognition domain of cd23 in the presence of glcnac-beta1-2-man
Structure deposition date
2019-07-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
E1BIQ4
Residue number A
174
Residue number B
177
Peptide name
Fc epsilon receptor II

Ligandability

Cysteine 174 of Fc epsilon receptor II

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 177 of Fc epsilon receptor II

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 Fc epsilon receptor II between cysteines 177 and 302 (165 and 290 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
6pwr
Structure name
crystal structure of the cow c-type carbohydrate-recognition domain of cd23 in the presence of glcnac-beta1-2-man
Structure deposition date
2019-07-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
E1BIQ4
Residue number A
177
Residue number B
302
Peptide name
Fc epsilon receptor II

Ligandability

Cysteine 177 of Fc epsilon receptor II

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 302 of Fc epsilon receptor II

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 Fc epsilon receptor II between cysteines 174 and 188 (162 and 176 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
6pwr
Structure name
crystal structure of the cow c-type carbohydrate-recognition domain of cd23 in the presence of glcnac-beta1-2-man
Structure deposition date
2019-07-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
E1BIQ4
Residue number A
174
Residue number B
188
Peptide name
Fc epsilon receptor II

Ligandability

Cysteine 174 of Fc epsilon receptor II

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 188 of Fc epsilon receptor II

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 Fc epsilon receptor II between cysteines 188 and 302 (176 and 290 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
6pwr
Structure name
crystal structure of the cow c-type carbohydrate-recognition domain of cd23 in the presence of glcnac-beta1-2-man
Structure deposition date
2019-07-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
E1BIQ4
Residue number A
188
Residue number B
302
Peptide name
Fc epsilon receptor II

Ligandability

Cysteine 188 of Fc epsilon receptor II

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 302 of Fc epsilon receptor II

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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