ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Glycine receptor subunit alpha-2

Intramolecular
Cysteine 232 and cysteine 243
Cysteine 172 and cysteine 186
Cysteine 75 and cysteine 232
Cysteine 75 and cysteine 243
A redox-regulated disulphide may form within Glycine receptor subunit alpha-2 between cysteines 232 and 243 (205 and 216 respectively in this structure).

Details

Redox score ?
77
PDB code
7kuy
Structure name
cyro-em structure of human glycine receptor alpha2-beta heteromer, strychnine bound state
Structure deposition date
2020-11-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
7
% buried
68
Peptide accession
P23416
Residue number A
232
Residue number B
243
Peptide name
Glycine receptor subunit alpha-2

Ligandability

Cysteine 232 of Glycine receptor subunit alpha-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 243 of Glycine receptor subunit alpha-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 Glycine receptor subunit alpha-2 between cysteines 172 and 186 (145 and 159 respectively in this structure).

Details

Redox score ?
74
PDB code
5bkg
Structure name
cyro-em structure of human glycine receptor alpha2-beta heteromer, glycine bound, (semi)open state
Structure deposition date
2021-03-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
8
% buried
84
Peptide accession
P23416
Residue number A
172
Residue number B
186
Peptide name
Glycine receptor subunit alpha-2

Ligandability

Cysteine 172 of Glycine receptor subunit alpha-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 186 of Glycine receptor subunit alpha-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 Glycine receptor subunit alpha-2 between cysteines 75 and 232 (48 and 205 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
5bkf
Structure name
cyro-em structure of human glycine receptor alpha2-beta heteromer, glycine bound, desensitized state
Structure deposition date
2021-03-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
12
% buried
nan
Peptide accession
P23416
Residue number A
75
Residue number B
232
Peptide name
Glycine receptor subunit alpha-2

Ligandability

Cysteine 75 of Glycine receptor subunit alpha-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 232 of Glycine receptor subunit alpha-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 Glycine receptor subunit alpha-2 between cysteines 75 and 243 (48 and 216 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
5bkf
Structure name
cyro-em structure of human glycine receptor alpha2-beta heteromer, glycine bound, desensitized state
Structure deposition date
2021-03-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
74
Minimum pKa ?
13
% buried
nan
Peptide accession
P23416
Residue number A
75
Residue number B
243
Peptide name
Glycine receptor subunit alpha-2

Ligandability

Cysteine 75 of Glycine receptor subunit alpha-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 243 of Glycine receptor subunit alpha-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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