Histone-lysine N-methyltransferase Smyd1
Intramolecular
Cysteine 65 and cysteine 68
Cysteine 274 and cysteine 279
Cysteine 208 and cysteine 279
Cysteine 276 and cysteine 279
Cysteine 68 and cysteine 90
Cysteine 74 and cysteine 78
Cysteine 52 and cysteine 78
Cysteine 65 and cysteine 90
Cysteine 55 and cysteine 78
Cysteine 274 and cysteine 276
More...Cysteine 208 and cysteine 274
Cysteine 55 and cysteine 74
Cysteine 52 and cysteine 55
Cysteine 208 and cysteine 276
Cysteine 332 and cysteine 335
Cysteine 52 and cysteine 74
3n71 A 65 A 68
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase Smyd1 between cysteines 65 and 68.
Details
Redox score ?
86
PDB code
3n71
Structure name
crystal structure of cardiac specific histone methyltransferase smyd1
Structure deposition date
2010-05-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
6
% buried
42
Peptide accession
Q6DFW7
Residue number A
65
Residue number B
68
Peptide name
Histone-lysine N-methyltransferase Smyd1
Ligandability
Cysteine 65 of Histone-lysine N-methyltransferase Smyd1
Cysteine 68 of Histone-lysine N-methyltransferase Smyd1
3n71 A 274 A 279
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase Smyd1 between cysteines 274 and 279.
Details
Redox score ?
84
PDB code
3n71
Structure name
crystal structure of cardiac specific histone methyltransferase smyd1
Structure deposition date
2010-05-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
6
% buried
57
Peptide accession
Q6DFW7
Residue number A
274
Residue number B
279
Peptide name
Histone-lysine N-methyltransferase Smyd1
Ligandability
Cysteine 274 of Histone-lysine N-methyltransferase Smyd1
Cysteine 279 of Histone-lysine N-methyltransferase Smyd1
3n71 A 208 A 279
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase Smyd1 between cysteines 208 and 279.
Details
Redox score ?
83
PDB code
3n71
Structure name
crystal structure of cardiac specific histone methyltransferase smyd1
Structure deposition date
2010-05-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
6
% buried
62
Peptide accession
Q6DFW7
Residue number A
208
Residue number B
279
Peptide name
Histone-lysine N-methyltransferase Smyd1
Ligandability
Cysteine 208 of Histone-lysine N-methyltransferase Smyd1
Cysteine 279 of Histone-lysine N-methyltransferase Smyd1
3n71 A 276 A 279
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase Smyd1 between cysteines 276 and 279.
Details
Redox score ?
82
PDB code
3n71
Structure name
crystal structure of cardiac specific histone methyltransferase smyd1
Structure deposition date
2010-05-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
6
% buried
nan
Peptide accession
Q6DFW7
Residue number A
276
Residue number B
279
Peptide name
Histone-lysine N-methyltransferase Smyd1
Ligandability
Cysteine 276 of Histone-lysine N-methyltransferase Smyd1
Cysteine 279 of Histone-lysine N-methyltransferase Smyd1
3n71 A 68 A 90
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase Smyd1 between cysteines 68 and 90.
Details
Redox score ?
80
PDB code
3n71
Structure name
crystal structure of cardiac specific histone methyltransferase smyd1
Structure deposition date
2010-05-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
6
% buried
42
Peptide accession
Q6DFW7
Residue number A
68
Residue number B
90
Peptide name
Histone-lysine N-methyltransferase Smyd1
Ligandability
Cysteine 68 of Histone-lysine N-methyltransferase Smyd1
Cysteine 90 of Histone-lysine N-methyltransferase Smyd1
3n71 A 74 A 78
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase Smyd1 between cysteines 74 and 78.
Details
Redox score ?
78
PDB code
3n71
Structure name
crystal structure of cardiac specific histone methyltransferase smyd1
Structure deposition date
2010-05-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
6
% buried
57
Peptide accession
Q6DFW7
Residue number A
74
Residue number B
78
Peptide name
Histone-lysine N-methyltransferase Smyd1
Ligandability
Cysteine 74 of Histone-lysine N-methyltransferase Smyd1
Cysteine 78 of Histone-lysine N-methyltransferase Smyd1
3n71 A 52 A 78
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase Smyd1 between cysteines 52 and 78.
Details
Redox score ?
78
PDB code
3n71
Structure name
crystal structure of cardiac specific histone methyltransferase smyd1
Structure deposition date
2010-05-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
6
% buried
nan
Peptide accession
Q6DFW7
Residue number A
52
Residue number B
78
Peptide name
Histone-lysine N-methyltransferase Smyd1
Ligandability
Cysteine 52 of Histone-lysine N-methyltransferase Smyd1
Cysteine 78 of Histone-lysine N-methyltransferase Smyd1
3n71 A 65 A 90
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase Smyd1 between cysteines 65 and 90.
Details
Redox score ?
77
PDB code
3n71
Structure name
crystal structure of cardiac specific histone methyltransferase smyd1
Structure deposition date
2010-05-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
7
% buried
31
Peptide accession
Q6DFW7
Residue number A
65
Residue number B
90
Peptide name
Histone-lysine N-methyltransferase Smyd1
Ligandability
Cysteine 65 of Histone-lysine N-methyltransferase Smyd1
Cysteine 90 of Histone-lysine N-methyltransferase Smyd1
3n71 A 55 A 78
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase Smyd1 between cysteines 55 and 78.
Details
Redox score ?
71
PDB code
3n71
Structure name
crystal structure of cardiac specific histone methyltransferase smyd1
Structure deposition date
2010-05-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
6
% buried
73
Peptide accession
Q6DFW7
Residue number A
55
Residue number B
78
Peptide name
Histone-lysine N-methyltransferase Smyd1
Ligandability
Cysteine 55 of Histone-lysine N-methyltransferase Smyd1
Cysteine 78 of Histone-lysine N-methyltransferase Smyd1
3n71 A 274 A 276
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase Smyd1 between cysteines 274 and 276.
Details
Redox score ?
67
PDB code
3n71
Structure name
crystal structure of cardiac specific histone methyltransferase smyd1
Structure deposition date
2010-05-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
14
% buried
nan
Peptide accession
Q6DFW7
Residue number A
274
Residue number B
276
Peptide name
Histone-lysine N-methyltransferase Smyd1
Ligandability
Cysteine 274 of Histone-lysine N-methyltransferase Smyd1
Cysteine 276 of Histone-lysine N-methyltransferase Smyd1
3n71 A 208 A 274
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase Smyd1 between cysteines 208 and 274.
Details
Redox score ?
64
PDB code
3n71
Structure name
crystal structure of cardiac specific histone methyltransferase smyd1
Structure deposition date
2010-05-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
14
% buried
68
Peptide accession
Q6DFW7
Residue number A
208
Residue number B
274
Peptide name
Histone-lysine N-methyltransferase Smyd1
Ligandability
Cysteine 208 of Histone-lysine N-methyltransferase Smyd1
Cysteine 274 of Histone-lysine N-methyltransferase Smyd1
3n71 A 55 A 74
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase Smyd1 between cysteines 55 and 74. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
3n71
Structure name
crystal structure of cardiac specific histone methyltransferase smyd1
Structure deposition date
2010-05-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
14
% buried
73
Peptide accession
Q6DFW7
Residue number A
55
Residue number B
74
Peptide name
Histone-lysine N-methyltransferase Smyd1
Ligandability
Cysteine 55 of Histone-lysine N-methyltransferase Smyd1
Cysteine 74 of Histone-lysine N-methyltransferase Smyd1
3n71 A 52 A 55
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase Smyd1 between cysteines 52 and 55. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
3n71
Structure name
crystal structure of cardiac specific histone methyltransferase smyd1
Structure deposition date
2010-05-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
86
Minimum pKa ?
14
% buried
nan
Peptide accession
Q6DFW7
Residue number A
52
Residue number B
55
Peptide name
Histone-lysine N-methyltransferase Smyd1
Ligandability
Cysteine 52 of Histone-lysine N-methyltransferase Smyd1
Cysteine 55 of Histone-lysine N-methyltransferase Smyd1
3n71 A 208 A 276
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase Smyd1 between cysteines 208 and 276. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
3n71
Structure name
crystal structure of cardiac specific histone methyltransferase smyd1
Structure deposition date
2010-05-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
22
% buried
nan
Peptide accession
Q6DFW7
Residue number A
208
Residue number B
276
Peptide name
Histone-lysine N-methyltransferase Smyd1
Ligandability
Cysteine 208 of Histone-lysine N-methyltransferase Smyd1
Cysteine 276 of Histone-lysine N-methyltransferase Smyd1
3n71 A 332 A 335
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase Smyd1 between cysteines 332 and 335. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
3n71
Structure name
crystal structure of cardiac specific histone methyltransferase smyd1
Structure deposition date
2010-05-26
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
10
% buried
68
Peptide accession
Q6DFW7
Residue number A
332
Residue number B
335
Peptide name
Histone-lysine N-methyltransferase Smyd1
Ligandability
Cysteine 332 of Histone-lysine N-methyltransferase Smyd1
Cysteine 335 of Histone-lysine N-methyltransferase Smyd1
3n71 A 52 A 74
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase Smyd1 between cysteines 52 and 74. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
3n71
Structure name
crystal structure of cardiac specific histone methyltransferase smyd1
Structure deposition date
2010-05-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
23
% buried
nan
Peptide accession
Q6DFW7
Residue number A
52
Residue number B
74
Peptide name
Histone-lysine N-methyltransferase Smyd1
Ligandability
Cysteine 52 of Histone-lysine N-methyltransferase Smyd1
Cysteine 74 of Histone-lysine N-methyltransferase Smyd1
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