a tool for identifying drug-targetable redox-active disulphides

tRNA (guanine-N(7)-)-methyltransferase

Intramolecular

Cysteine 85 and cysteine 136

A redox-regulated disulphide may form within tRNA (guanine-N(7)-)-methyltransferase between cysteines 85 and 136.

Details

Redox score ?

71

PDB code

Structure name

crystal structure of human mettl1-wdr4 complex

Structure deposition date

2022-06-04

Thiol separation (Å)

4

Half-sphere exposure sum ?

88

Minimum pK_a ?

9

% buried

91

Peptide accession

Residue number A

85

Residue number B

136

Peptide name

tRNA (guanine-N(7)-)-methyltransferase

Ligandability

Cysteine 85 of tRNA (guanine-N(7)-)-methyltransferase

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 136 of tRNA (guanine-N(7)-)-methyltransferase

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.

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