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

Intermolecular

Cysteine 140 of Rhodopsin and cysteine 347

A redox-regulated disulphide may form between two units of Guanine nucleotide-binding protein G(t) subunit alpha-1 at cysteines 210 and 62. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

1tnd

Structure name

the 2

Structure deposition date

1994-03-31

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

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

Peptide B name

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

Peptide A accession

P04695

Peptide B accession

P04695

Peptide A residue number

210

Peptide B residue number

Ligandability

Cysteine 210 of Guanine nucleotide-binding protein G(t) 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 62 of Guanine nucleotide-binding protein G(t) 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.

A redox-regulated disulphide may form between cysteine 140 of Rhodopsin and cysteine 347 of Guanine nucleotide-binding protein G(t) subunit alpha-1. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?