a tool for identifying drug-targetable redox-active disulphides

Myelin P2 protein

Intramolecular

Cysteine 118 and cysteine 125

A redox-regulated disulphide may form within Myelin P2 protein between cysteines 118 and 125 (117 and 124 respectively in this structure).

Details

Redox score ?

76

PDB code

Structure name

human myelin protein p2 f57a mutant, monoclinic crystal form

Structure deposition date

2017-11-03

Thiol separation (Å)

3

Half-sphere exposure sum ?

64

Minimum pK_a ?

nan

% buried

56

Peptide accession

Residue number A

118

Residue number B

125

Peptide name

Myelin P2 protein

Ligandability

Cysteine 118 of Myelin P2 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 125 of Myelin P2 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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