a tool for identifying drug-targetable redox-active disulphides

Major prion protein

Intramolecular

Cysteine 182 and cysteine 217

A redox-regulated disulphide may form within Major prion protein between cysteines 182 and 217.

Details

Redox score ?

83

PDB code

Structure name

solution nmr structure of h2h3 domain of ovine prion protein (residues 167-234)

Structure deposition date

2010-02-04

Thiol separation (Å)

2

Half-sphere exposure sum ?

60

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

182

Residue number B

217

Peptide name

Major prion protein

Ligandability

Cysteine 182 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 217 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.

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