a tool for identifying drug-targetable redox-active disulphides

Uncharacterized protein

Intramolecular

Cysteine 273 and cysteine 313

A redox-regulated disulphide may form within Uncharacterized protein between cysteines 273 and 313 (217 and 257 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

53

PDB code

Structure name

cardiac thin filament decorated with regulatory m-domain of cardiac myosin binding protein c

Structure deposition date

2022-01-14

Thiol separation (Å)

6

Half-sphere exposure sum ?

77

Minimum pK_a ?

12

% buried

98

Peptide accession

Residue number A

273

Residue number B

313

Peptide name

Uncharacterized protein

Ligandability

Cysteine 273 of Uncharacterized protein

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 313 of Uncharacterized protein

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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