a tool for identifying drug-targetable redox-active disulphides

Actin, cytoplasmic 2

Intramolecular

Cysteine 217 and cysteine 257

A redox-regulated disulphide may form within Actin, cytoplasmic 2 between cysteines 217 and 257 (216 and 256 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

54

PDB code

Structure name

cardiac thin filament decorated with c0c1 fragment of cardiac myosin binding protein c mode 1

Structure deposition date

2018-04-03

Thiol separation (Å)

6

Half-sphere exposure sum ?

77

Minimum pK_a ?

12

% buried

96

Peptide accession

Residue number A

217

Residue number B

257

Peptide name

Actin, cytoplasmic 2

Ligandability

Cysteine 217 of Actin, cytoplasmic 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 257 of Actin, cytoplasmic 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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