ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Acetylcholine receptor subunit alpha

Intramolecular
Cysteine 148 and cysteine 162
Cysteine 212 and cysteine 213
A redox-regulated disulphide may form within Acetylcholine receptor subunit alpha between cysteines 148 and 162 (128 and 142 respectively in this structure).

Details

Redox score ?
85
PDB code
2qc1
Structure name
crystal structure of the extracellular domain of the nicotinic acetylcholine receptor 1 subunit bound to alpha-bungarotoxin at 1
Structure deposition date
2007-06-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04756
Residue number A
148
Residue number B
162
Peptide name
Acetylcholine receptor subunit alpha

Ligandability

Cysteine 148 of Acetylcholine receptor subunit alpha

Cysteine 162 of Acetylcholine receptor subunit alpha

A redox-regulated disulphide may form within Acetylcholine receptor subunit alpha between cysteines 212 and 213 (192 and 193 respectively in this structure).

Details

Redox score ?
83
PDB code
5hbv
Structure name
complex structure of fab35 and mouse nachr alpha1
Structure deposition date
2016-01-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04756
Residue number A
212
Residue number B
213
Peptide name
Acetylcholine receptor subunit alpha

Ligandability

Cysteine 212 of Acetylcholine receptor subunit alpha

Cysteine 213 of Acetylcholine receptor subunit alpha

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