ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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High affinity immunoglobulin epsilon receptor subunit alpha

Intramolecular
Cysteine 51 and cysteine 93
Cysteine 132 and cysteine 176
A redox-regulated disulphide may form within High affinity immunoglobulin epsilon receptor subunit alpha between cysteines 51 and 93 (26 and 68 respectively in this structure).

Details

Redox score ?
81
PDB code
1j89
Structure name
human high affinity fc receptor fc(epsilon)ri(alpha), tetragonal crystal form 2
Structure deposition date
2001-05-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
P12319
Residue number A
51
Residue number B
93
Peptide name
High affinity immunoglobulin epsilon receptor subunit alpha

Ligandability

Cysteine 51 of High affinity immunoglobulin epsilon receptor subunit alpha

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 High affinity immunoglobulin epsilon receptor subunit alpha

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 High affinity immunoglobulin epsilon receptor subunit alpha between cysteines 132 and 176 (107 and 151 respectively in this structure).

Details

Redox score ?
81
PDB code
1j89
Structure name
human high affinity fc receptor fc(epsilon)ri(alpha), tetragonal crystal form 2
Structure deposition date
2001-05-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
91
Minimum pKa ?
nan
% buried
nan
Peptide accession
P12319
Residue number A
132
Residue number B
176
Peptide name
High affinity immunoglobulin epsilon receptor subunit alpha

Ligandability

Cysteine 132 of High affinity immunoglobulin epsilon receptor subunit alpha

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 176 of High affinity immunoglobulin epsilon receptor subunit alpha

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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