a tool for identifying drug-targetable redox-active disulphides

tRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit TRM6

Intramolecular

Cysteine 401 and cysteine 410

A redox-regulated disulphide may form within tRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit TRM6 between cysteines 401 and 410. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

35

PDB code

Structure name

crystal structure of human m1a58 methyltransferase in a complex with trna3lys and sah

Structure deposition date

2015-07-01

Thiol separation (Å)

9

Half-sphere exposure sum ?

78

Minimum pK_a ?

11

% buried

73

Peptide accession

Residue number A

401

Residue number B

410

Peptide name

tRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit TRM6

Ligandability

Cysteine 401 of tRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit TRM6

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 410 of tRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit TRM6

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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