a tool for identifying drug-targetable redox-active disulphides

Urotensin-2

Intramolecular

Cysteine 118 and cysteine 123

A redox-regulated disulphide may form within Urotensin-2 between cysteines 118 and 123 (5 and 10 respectively in this structure).

Details

Redox score ?

91

PDB code

Structure name

nmr structure of urotensin peptide asp-c[cys-phe-(n-me)trp-lys-tyr- cys]-val in sds solution

Structure deposition date

2018-10-10

Thiol separation (Å)

2

Half-sphere exposure sum ?

12

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

118

Residue number B

123

Peptide name

Urotensin-2

Ligandability

Cysteine 118 of Urotensin-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 123 of Urotensin-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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