a tool for identifying drug-targetable redox-active disulphides

Protocadherin-1

Intramolecular

Cysteine 123 and cysteine 132

A redox-regulated disulphide may form within Protocadherin-1 between cysteines 123 and 132 (66 and 75 respectively in this structure).

Details

Redox score ?

87

PDB code

Structure name

crystal structure of human protocadherin 1 ec1-ec4

Structure deposition date

2020-01-06

Thiol separation (Å)

2

Half-sphere exposure sum ?

58

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

123

Residue number B

132

Peptide name

Protocadherin-1

Ligandability

Cysteine 123 of Protocadherin-1

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 132 of Protocadherin-1

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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