a tool for identifying drug-targetable redox-active disulphides

Major prion protein

Intramolecular

Cysteine 178 and cysteine 213

A redox-regulated disulphide may form within Major prion protein between cysteines 178 and 213 (179 and 214 respectively in this structure).

Details

Redox score ?

82

PDB code

Structure name

mouse prion protein (121-231) containing the substitution f175a

Structure deposition date

2010-07-28

Thiol separation (Å)

2

Half-sphere exposure sum ?

86

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

178

Residue number B

213

Peptide name

Major prion protein

Ligandability

Cysteine 178 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 213 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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