ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Gamma-aminobutyric acid type A receptor subunit gamma2

Intramolecular
Cysteine 161 and cysteine 175
Cysteine 254 and cysteine 313
A redox-regulated disulphide may form within Gamma-aminobutyric acid type A receptor subunit gamma2 between cysteines 161 and 175 (151 and 165 respectively in this structure).

Details

Redox score ?
83
PDB code
7qnb
Structure name
cryo-em structure of human full-length beta3gamma2 gaba(a)r in complex with gaba and nanobody nb25
Structure deposition date
2021-12-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
A0A2K5TLN2
Residue number A
161
Residue number B
175
Peptide name
Gamma-aminobutyric acid type A receptor subunit gamma2

Ligandability

Cysteine 161 of Gamma-aminobutyric acid type A receptor subunit gamma2

Cysteine 175 of Gamma-aminobutyric acid type A receptor subunit gamma2

A redox-regulated disulphide may form within Gamma-aminobutyric acid type A receptor subunit gamma2 between cysteines 254 and 313 (244 and 303 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
7qnb
Structure name
cryo-em structure of human full-length beta3gamma2 gaba(a)r in complex with gaba and nanobody nb25
Structure deposition date
2021-12-20
Thiol separation (Å)
5
Half-sphere exposure sum ?
84
Minimum pKa ?
12
% buried
97
Peptide accession
A0A2K5TLN2
Residue number A
254
Residue number B
313
Peptide name
Gamma-aminobutyric acid type A receptor subunit gamma2

Ligandability

Cysteine 254 of Gamma-aminobutyric acid type A receptor subunit gamma2

Cysteine 313 of Gamma-aminobutyric acid type A receptor subunit gamma2

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