Probable tRNA(His) guanylyltransferase

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of Probable tRNA(His) guanylyltransferase at cysteines 51 and 51 (22 and 22 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

7cv1

Structure name

structure of human trnahis guanylyltransferase (thg1) in the presence of human mitochondrial trnahis

Structure deposition date

2020-08-25

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

Probable tRNA(His) guanylyltransferase

Peptide B name

Probable tRNA(His) guanylyltransferase

Peptide A accession

Q9NWX6

Peptide B accession

Q9NWX6

Peptide A residue number

Peptide B residue number

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 Probable tRNA(His) guanylyltransferase between cysteines 47 and 51 (18 and 22 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?