a tool for identifying drug-targetable redox-active disulphides

Mucin 16

Intramolecular

Cysteine 123 and cysteine 144

A redox-regulated disulphide may form within Mucin 16 between cysteines 123 and 144 (64 and 85 respectively in this structure).

Details

Redox score ?

66

PDB code

Structure name

solution structure of the sea domain from murine hypothetical protein homologous to human mucin 16

Structure deposition date

2002-04-02

Thiol separation (Å)

4

Half-sphere exposure sum ?

77

Minimum pK_a ?

10

% buried

92

Peptide accession

Residue number A

123

Residue number B

144

Peptide name

Mucin 16

Ligandability

Cysteine 123 of Mucin 16

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 144 of Mucin 16

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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