a tool for identifying drug-targetable redox-active disulphides

Renin-1

Intramolecular

Cysteine 278 and cysteine 282

A redox-regulated disulphide may form within Renin-1 between cysteines 278 and 282 (257 and 261 respectively in this structure).

Details

Redox score ?

85

PDB code

Structure name

crystal structure of mouse prorenin

Structure deposition date

2016-12-05

Thiol separation (Å)

2

Half-sphere exposure sum ?

57

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

278

Residue number B

282

Peptide name

Renin-1

Ligandability

Cysteine 278 of Renin-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 282 of Renin-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.

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