Protein arginine N-methyltransferase 1
1orh A 232 A 254
A redox-regulated disulphide may form within Protein arginine N-methyltransferase 1 between cysteines 232 and 254.
Details
Redox score ?
64
PDB code
1orh
Structure name
structure of the predominant protein arginine methyltransferase prmt1
Structure deposition date
2003-03-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
15
Peptide accession
Q63009
Residue number A
232
Residue number B
254
Peptide name
Protein arginine N-methyltransferase 1
Ligandability
Cysteine 232 of Protein arginine N-methyltransferase 1
Cysteine 254 of Protein arginine N-methyltransferase 1
3q7e A 342 A 346
A redox-regulated disulphide may form within Protein arginine N-methyltransferase 1 between cysteines 342 and 346. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
3q7e
Structure name
crystal structure of rat protein arginine methyltransferase 1 (prmt1) m48l mutant
Structure deposition date
2011-01-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
43
Minimum pKa ?
9
% buried
32
Peptide accession
Q63009
Residue number A
342
Residue number B
346
Peptide name
Protein arginine N-methyltransferase 1
Ligandability
Cysteine 342 of Protein arginine N-methyltransferase 1
Cysteine 346 of Protein arginine N-methyltransferase 1
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