a tool for identifying drug-targetable redox-active disulphides

Myelin protein P0

Intramolecular

Cysteine 50 and cysteine 127

A redox-regulated disulphide may form within Myelin protein P0 between cysteines 50 and 127 (1021 and 1098 respectively in this structure).

Details

Redox score ?

82

PDB code

Structure name

crystal structure of the extra-cellular domain of human myelin protein zero

Structure deposition date

2010-08-05

Thiol separation (Å)

2

Half-sphere exposure sum ?

78

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

50

Residue number B

127

Peptide name

Myelin protein P0

Ligandability

Cysteine 50 of Myelin protein P0

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 127 of Myelin protein P0

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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