Trimethylguanosine synthase

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of Trimethylguanosine synthase at cysteines 745 and 745. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

3egi

Structure name

methyltransferase domain of human trimethylguanosine synthase tgs1 bound to m7gpppa (inactive form)

Structure deposition date

2008-09-10

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

Trimethylguanosine synthase

Peptide B name

Trimethylguanosine synthase

Peptide A accession

Q96RS0

Peptide B accession

Q96RS0

Peptide A residue number

745

Peptide B residue number

745

Ligandability

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.

A redox-regulated disulphide may form within Trimethylguanosine synthase between cysteines 699 and 745. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?