a tool for identifying drug-targetable redox-active disulphides

Coiled-coil domain containing 142

Intramolecular

Cysteine 516 and cysteine 119

A redox-regulated disulphide may form within Coiled-coil domain containing 142 between cysteines 516 and 119 (21 and 63 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

37

PDB code

Structure name

structure of the large subunit of the mammalian mitoribosome, part 2 of 2

Structure deposition date

2014-09-25

Thiol separation (Å)

10

Half-sphere exposure sum ?

64

Minimum pK_a ?

9

% buried

26

Peptide accession

Residue number A

516

Residue number B

119

Peptide name

Coiled-coil domain containing 142

Ligandability

Cysteine 516 of Coiled-coil domain containing 142

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 119 of Coiled-coil domain containing 142

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.

Uncertain whether structure cysteine 63 has been assigned to correct residue.

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