Protein arginine N-methyltransferase 9

Intramolecular

A redox-regulated disulphide may form within Protein arginine N-methyltransferase 9 between cysteines 459 and 462. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

7rbq

Structure name

co-crystal structure of human prmt9 in complex with mt556 inhibitor

Structure deposition date

2021-07-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Q6P2P2

Residue number A

459

Residue number B

462

Peptide name

Protein arginine N-methyltransferase 9

Ligandability

Cysteine 459 of Protein arginine N-methyltransferase 9

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.