a tool for identifying drug-targetable redox-active disulphides

Guanine nucleotide-binding protein G(t) subunit alpha-2

Intermolecular

Cysteine 122 of Synembryn-A and cysteine 351

A redox-regulated disulphide may form between cysteine 122 of Synembryn-A and cysteine 351 of Guanine nucleotide-binding protein G(t) subunit alpha-2 (122 and 392 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

41

PDB code

Structure name

resistance to inhibitors of cholinesterase 8a (ric8a) protein in complex with mbp-tagged transducin-alpha residues 327-350

Structure deposition date

2018-11-28

Thiol separation (Å)

9

Half-sphere exposure sum ?

65

Minimum pK_a ?

11

% buried

86

Peptide A name

Synembryn-A

Peptide B name

Guanine nucleotide-binding protein G(t) subunit alpha-2

Peptide A accession

Peptide B accession

Peptide A residue number

122

Peptide B residue number

351

Ligandability

Cysteine 122 of Synembryn-A

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 351 of Guanine nucleotide-binding protein G(t) 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.

If this tool was useful for finding a disulphide, please cite: