a tool for identifying drug-targetable redox-active disulphides

Major prion protein

Intramolecular

Cysteine 166 and cysteine 201

A redox-regulated disulphide may form within Major prion protein between cysteines 166 and 201 (179 and 214 respectively in this structure).

Details

Redox score ?

81

PDB code

Structure name

horse prion protein

Structure deposition date

2010-02-12

Thiol separation (Å)

2

Half-sphere exposure sum ?

85

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

166

Residue number B

201

Peptide name

Major prion protein

Ligandability

Cysteine 166 of Major prion 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 201 of Major prion 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.

If this tool was useful for finding a disulphide, please cite: