a tool for identifying drug-targetable redox-active disulphides

Renin-2

Intramolecular

Cysteine 320 and cysteine 357

A redox-regulated disulphide may form within Renin-2 between cysteines 320 and 357 (249 and 282 respectively in this structure).

Details

Redox score ?

86

PDB code

Structure name

the 3-d structure of mouse submaxillary renin complexed with a decapeptide inhibitor ch-66 based on the 4-16 fragment of rat angiotensinogen

Structure deposition date

1992-03-11

Thiol separation (Å)

2

Half-sphere exposure sum ?

49

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

320

Residue number B

357

Peptide name

Renin-2

Ligandability

Cysteine 320 of Renin-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.

Cysteine 357 of Renin-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.

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