Protein arginine N-methyltransferase 2

Intramolecular

A redox-regulated disulphide may form within Protein arginine N-methyltransferase 2 between cysteines 264 and 311. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

5fwd

Structure name

crystal structure of mus musculus protein arginine methyltransferase 2 with cp2

Structure deposition date

2016-02-12

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Q3UKX1

Residue number A

264

Residue number B

311

Peptide name

Protein arginine N-methyltransferase 2

Ligandability

Cysteine 264 of Protein arginine N-methyltransferase 2

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.