Protein arginine N-methyltransferase 3
Intramolecular
Cysteine 48 and cysteine 51
Cysteine 48 and cysteine 65
Cysteine 363 and cysteine 424
Cysteine 51 and cysteine 65
1wir A 18 A 21
A redox-regulated disulphide may form within Protein arginine N-methyltransferase 3 between cysteines 48 and 51 (18 and 21 respectively in this structure).
Details
Redox score ?
91
PDB code
1wir
Structure name
solution structure of the c2h2 zinc finger domain of the protein arginine n-methyltransferase 3 from mus musculus
Structure deposition date
2004-05-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
3
% buried
32
Peptide accession
Q922H1
Residue number A
48
Residue number B
51
Peptide name
Protein arginine N-methyltransferase 3
Ligandability
Cysteine 48 of Protein arginine N-methyltransferase 3
Cysteine 51 of Protein arginine N-methyltransferase 3
1wir A 18 A 35
A redox-regulated disulphide may form within Protein arginine N-methyltransferase 3 between cysteines 48 and 65 (18 and 35 respectively in this structure).
Details
Redox score ?
90
PDB code
1wir
Structure name
solution structure of the c2h2 zinc finger domain of the protein arginine n-methyltransferase 3 from mus musculus
Structure deposition date
2004-05-28
Thiol separation (Å)
3
Half-sphere exposure sum ?
61
Minimum pKa ?
3
% buried
53
Peptide accession
Q922H1
Residue number A
48
Residue number B
65
Peptide name
Protein arginine N-methyltransferase 3
Ligandability
Cysteine 48 of Protein arginine N-methyltransferase 3
Cysteine 65 of Protein arginine N-methyltransferase 3
2fyt A 380 A 441
A redox-regulated disulphide may form within Protein arginine N-methyltransferase 3 between cysteines 363 and 424 (380 and 441 respectively in this structure).
Details
Redox score ?
71
PDB code
2fyt
Structure name
human hmt1 hnrnp methyltransferase-like 3 (s
Structure deposition date
2006-02-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
9
% buried
100
Peptide accession
O60678
Residue number A
363
Residue number B
424
Peptide name
Protein arginine N-methyltransferase 3
Ligandability
Cysteine 363 of Protein arginine N-methyltransferase 3
Cysteine 424 of Protein arginine N-methyltransferase 3
1wir A 21 A 35
A redox-regulated disulphide may form within Protein arginine N-methyltransferase 3 between cysteines 51 and 65 (21 and 35 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
1wir
Structure name
solution structure of the c2h2 zinc finger domain of the protein arginine n-methyltransferase 3 from mus musculus
Structure deposition date
2004-05-28
Thiol separation (Å)
6
Half-sphere exposure sum ?
48
Minimum pKa ?
10
% buried
35
Peptide accession
Q922H1
Residue number A
51
Residue number B
65
Peptide name
Protein arginine N-methyltransferase 3
Ligandability
Cysteine 51 of Protein arginine N-methyltransferase 3
Cysteine 65 of Protein arginine N-methyltransferase 3
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