a tool for identifying drug-targetable redox-active disulphides

Selenoprotein M

Intramolecular

Cysteine 45 and cysteine 48

A redox-regulated disulphide may form within Selenoprotein M between cysteines 45 and 48.

Details

Redox score ?

86

PDB code

Structure name

solution structure of selm from mus musculus

Structure deposition date

2005-06-22

Thiol separation (Å)

2

Half-sphere exposure sum ?

39

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

45

Residue number B

48

Peptide name

Selenoprotein M

Ligandability

Cysteine 45 of Selenoprotein M

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 48 of Selenoprotein M

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 48 in protein B could not be asigned to a Uniprot residue.

If this tool was useful for finding a disulphide, please cite: