Inactive histone-lysine N-methyltransferase 2E
Intramolecular
Cysteine 121 and cysteine 123
Cysteine 135 and cysteine 163
Cysteine 121 and cysteine 146
Cysteine 135 and cysteine 138
Cysteine 160 and cysteine 163
Cysteine 135 and cysteine 160
Cysteine 138 and cysteine 160
Cysteine 138 and cysteine 163
Cysteine 123 and cysteine 146
Cysteine 134 and cysteine 135
More...Cysteine 121 and cysteine 160
Cysteine 134 and cysteine 138
Cysteine 134 and cysteine 160
4l58 A 5 A 7
A redox-regulated disulphide may form within Inactive histone-lysine N-methyltransferase 2E between cysteines 121 and 123 (5 and 7 respectively in this structure).
Details
Redox score ?
91
PDB code
4l58
Structure name
crystal structure of the mll5 phd finger in complex with h3k4me3
Structure deposition date
2013-06-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
2
% buried
54
Peptide accession
Q8IZD2
Residue number A
121
Residue number B
123
Peptide name
Inactive histone-lysine N-methyltransferase 2E
Ligandability
Cysteine 121 of Inactive histone-lysine N-methyltransferase 2E
Cysteine 123 of Inactive histone-lysine N-methyltransferase 2E
4l58 A 19 A 47
A redox-regulated disulphide may form within Inactive histone-lysine N-methyltransferase 2E between cysteines 135 and 163 (19 and 47 respectively in this structure).
Details
Redox score ?
90
PDB code
4l58
Structure name
crystal structure of the mll5 phd finger in complex with h3k4me3
Structure deposition date
2013-06-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
5
% buried
6
Peptide accession
Q8IZD2
Residue number A
135
Residue number B
163
Peptide name
Inactive histone-lysine N-methyltransferase 2E
Ligandability
Cysteine 135 of Inactive histone-lysine N-methyltransferase 2E
Cysteine 163 of Inactive histone-lysine N-methyltransferase 2E
4l58 A 5 A 30
A redox-regulated disulphide may form within Inactive histone-lysine N-methyltransferase 2E between cysteines 121 and 146 (5 and 30 respectively in this structure).
Details
Redox score ?
89
PDB code
4l58
Structure name
crystal structure of the mll5 phd finger in complex with h3k4me3
Structure deposition date
2013-06-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
2
% buried
60
Peptide accession
Q8IZD2
Residue number A
121
Residue number B
146
Peptide name
Inactive histone-lysine N-methyltransferase 2E
Ligandability
Cysteine 121 of Inactive histone-lysine N-methyltransferase 2E
Cysteine 146 of Inactive histone-lysine N-methyltransferase 2E
4l58 A 19 A 22
A redox-regulated disulphide may form within Inactive histone-lysine N-methyltransferase 2E between cysteines 135 and 138 (19 and 22 respectively in this structure).
Details
Redox score ?
87
PDB code
4l58
Structure name
crystal structure of the mll5 phd finger in complex with h3k4me3
Structure deposition date
2013-06-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
5
% buried
8
Peptide accession
Q8IZD2
Residue number A
135
Residue number B
138
Peptide name
Inactive histone-lysine N-methyltransferase 2E
Ligandability
Cysteine 135 of Inactive histone-lysine N-methyltransferase 2E
Cysteine 138 of Inactive histone-lysine N-methyltransferase 2E
4l58 A 44 A 47
A redox-regulated disulphide may form within Inactive histone-lysine N-methyltransferase 2E between cysteines 160 and 163 (44 and 47 respectively in this structure).
Details
Redox score ?
86
PDB code
4l58
Structure name
crystal structure of the mll5 phd finger in complex with h3k4me3
Structure deposition date
2013-06-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
7
% buried
8
Peptide accession
Q8IZD2
Residue number A
160
Residue number B
163
Peptide name
Inactive histone-lysine N-methyltransferase 2E
Ligandability
Cysteine 160 of Inactive histone-lysine N-methyltransferase 2E
Cysteine 163 of Inactive histone-lysine N-methyltransferase 2E
4l58 A 19 A 44
A redox-regulated disulphide may form within Inactive histone-lysine N-methyltransferase 2E between cysteines 135 and 160 (19 and 44 respectively in this structure).
Details
Redox score ?
86
PDB code
4l58
Structure name
crystal structure of the mll5 phd finger in complex with h3k4me3
Structure deposition date
2013-06-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
5
% buried
14
Peptide accession
Q8IZD2
Residue number A
135
Residue number B
160
Peptide name
Inactive histone-lysine N-methyltransferase 2E
Ligandability
Cysteine 135 of Inactive histone-lysine N-methyltransferase 2E
Cysteine 160 of Inactive histone-lysine N-methyltransferase 2E
4l58 A 22 A 44
A redox-regulated disulphide may form within Inactive histone-lysine N-methyltransferase 2E between cysteines 138 and 160 (22 and 44 respectively in this structure).
Details
Redox score ?
83
PDB code
4l58
Structure name
crystal structure of the mll5 phd finger in complex with h3k4me3
Structure deposition date
2013-06-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
7
% buried
11
Peptide accession
Q8IZD2
Residue number A
138
Residue number B
160
Peptide name
Inactive histone-lysine N-methyltransferase 2E
Ligandability
Cysteine 138 of Inactive histone-lysine N-methyltransferase 2E
Cysteine 160 of Inactive histone-lysine N-methyltransferase 2E
4l58 A 22 A 47
A redox-regulated disulphide may form within Inactive histone-lysine N-methyltransferase 2E between cysteines 138 and 163 (22 and 47 respectively in this structure).
Details
Redox score ?
81
PDB code
4l58
Structure name
crystal structure of the mll5 phd finger in complex with h3k4me3
Structure deposition date
2013-06-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
35
Minimum pKa ?
9
% buried
2
Peptide accession
Q8IZD2
Residue number A
138
Residue number B
163
Peptide name
Inactive histone-lysine N-methyltransferase 2E
Ligandability
Cysteine 138 of Inactive histone-lysine N-methyltransferase 2E
Cysteine 163 of Inactive histone-lysine N-methyltransferase 2E
4l58 A 7 A 30
A redox-regulated disulphide may form within Inactive histone-lysine N-methyltransferase 2E between cysteines 123 and 146 (7 and 30 respectively in this structure).
Details
Redox score ?
75
PDB code
4l58
Structure name
crystal structure of the mll5 phd finger in complex with h3k4me3
Structure deposition date
2013-06-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
44
Peptide accession
Q8IZD2
Residue number A
123
Residue number B
146
Peptide name
Inactive histone-lysine N-methyltransferase 2E
Ligandability
Cysteine 123 of Inactive histone-lysine N-methyltransferase 2E
Cysteine 146 of Inactive histone-lysine N-methyltransferase 2E
4l58 A 18 A 19
A redox-regulated disulphide may form within Inactive histone-lysine N-methyltransferase 2E between cysteines 134 and 135 (18 and 19 respectively in this structure).
Details
Redox score ?
65
PDB code
4l58
Structure name
crystal structure of the mll5 phd finger in complex with h3k4me3
Structure deposition date
2013-06-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
62
Minimum pKa ?
5
% buried
15
Peptide accession
Q8IZD2
Residue number A
134
Residue number B
135
Peptide name
Inactive histone-lysine N-methyltransferase 2E
Ligandability
Cysteine 134 of Inactive histone-lysine N-methyltransferase 2E
Cysteine 135 of Inactive histone-lysine N-methyltransferase 2E
4l58 A 5 A 44
A redox-regulated disulphide may form within Inactive histone-lysine N-methyltransferase 2E between cysteines 121 and 160 (5 and 44 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
4l58
Structure name
crystal structure of the mll5 phd finger in complex with h3k4me3
Structure deposition date
2013-06-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
68
Minimum pKa ?
2
% buried
43
Peptide accession
Q8IZD2
Residue number A
121
Residue number B
160
Peptide name
Inactive histone-lysine N-methyltransferase 2E
Ligandability
Cysteine 121 of Inactive histone-lysine N-methyltransferase 2E
Cysteine 160 of Inactive histone-lysine N-methyltransferase 2E
4l58 A 18 A 22
A redox-regulated disulphide may form within Inactive histone-lysine N-methyltransferase 2E between cysteines 134 and 138 (18 and 22 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
4l58
Structure name
crystal structure of the mll5 phd finger in complex with h3k4me3
Structure deposition date
2013-06-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
12
Peptide accession
Q8IZD2
Residue number A
134
Residue number B
138
Peptide name
Inactive histone-lysine N-methyltransferase 2E
Ligandability
Cysteine 134 of Inactive histone-lysine N-methyltransferase 2E
Cysteine 138 of Inactive histone-lysine N-methyltransferase 2E
4l58 A 18 A 44
A redox-regulated disulphide may form within Inactive histone-lysine N-methyltransferase 2E between cysteines 134 and 160 (18 and 44 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
4l58
Structure name
crystal structure of the mll5 phd finger in complex with h3k4me3
Structure deposition date
2013-06-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
7
% buried
18
Peptide accession
Q8IZD2
Residue number A
134
Residue number B
160
Peptide name
Inactive histone-lysine N-methyltransferase 2E
Ligandability
Cysteine 134 of Inactive histone-lysine N-methyltransferase 2E
Cysteine 160 of Inactive histone-lysine N-methyltransferase 2E
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