ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Protein arginine N-methyltransferase 6

Intermolecular
Cysteine 232 and cysteine 53
Intramolecular
Cysteine 280 and cysteine 282
A redox-regulated disulphide may form between two units of Protein arginine N-methyltransferase 6 at cysteines 232 and 53.

Details

Redox score ?
87
PDB code
6sqh
Structure name
crystal structure of mouse prmt6 with partial c-terminal tev cleavage site
Structure deposition date
2019-09-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide A name
Protein arginine N-methyltransferase 6
Peptide B name
Protein arginine N-methyltransferase 6
Peptide A accession
Q6NZB1
Peptide B accession
Q6NZB1
Peptide A residue number
232
Peptide B residue number
53

Ligandability

Cysteine 232 of Protein arginine N-methyltransferase 6

Cysteine 53 of Protein arginine N-methyltransferase 6

A redox-regulated disulphide may form within Protein arginine N-methyltransferase 6 between cysteines 280 and 282. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
4c04
Structure name
crystal structure of m
Structure deposition date
2013-07-31
Thiol separation (Å)
6
Half-sphere exposure sum ?
61
Minimum pKa ?
11
% buried
54
Peptide accession
Q6NZB1
Residue number A
280
Residue number B
282
Peptide name
Protein arginine N-methyltransferase 6

Ligandability

Cysteine 280 of Protein arginine N-methyltransferase 6

Cysteine 282 of Protein arginine N-methyltransferase 6

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