a tool for identifying drug-targetable redox-active disulphides

Prostacyclin receptor

Intramolecular

Cysteine 412 and cysteine 415

A redox-regulated disulphide may form within Prostacyclin receptor between cysteines 412 and 415 (110 and 113 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

48

PDB code

Structure name

molecular analysis of the interaction between the prostacyclin receptor and the first pdz domain of pdzk1

Structure deposition date

2012-05-17

Thiol separation (Å)

9

Half-sphere exposure sum ?

nan

Minimum pK_a ?

9

% buried

40

Peptide accession

Residue number A

412

Residue number B

415

Peptide name

Prostacyclin receptor

Ligandability

Cysteine 412 of Prostacyclin receptor

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 415 of Prostacyclin receptor

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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