a tool for identifying drug-targetable redox-active disulphides

5-hydroxytryptamine receptor 4

Intermolecular

Cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1 and cysteine 123

A redox-regulated disulphide may form between cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1 and cysteine 123 of 5-hydroxytryptamine receptor 4 (351 and 122 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

33

PDB code

Structure name

serotonin 4 (5-ht4) receptor-gi-scfv16 complex

Structure deposition date

2022-05-16

Thiol separation (Å)

10

Half-sphere exposure sum ?

70

Minimum pK_a ?

10

% buried

74

Peptide A name

Guanine nucleotide-binding protein G(i) subunit alpha-1

Peptide B name

5-hydroxytryptamine receptor 4

Peptide A accession

Peptide B accession

Peptide A residue number

351

Peptide B residue number

123

Ligandability

Cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1

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 123 of 5-hydroxytryptamine receptor 4

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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