Histone-lysine N-methyltransferase EHMT2
Intramolecular
Cysteine 426 and cysteine 428
Cysteine 1115 and cysteine 1170
Cysteine 1023 and cysteine 1027
Cysteine 1115 and cysteine 1175
Cysteine 1170 and cysteine 1175
Cysteine 446 and cysteine 459
Cysteine 1168 and cysteine 1175
Cysteine 459 and cysteine 481
Cysteine 974 and cysteine 1021
Cysteine 1168 and cysteine 1170
More...Cysteine 976 and cysteine 980
Cysteine 974 and cysteine 987
Cysteine 446 and cysteine 481
Cysteine 974 and cysteine 980
Cysteine 937 and cysteine 946
Cysteine 987 and cysteine 1023
Cysteine 974 and cysteine 1023
Cysteine 976 and cysteine 985
Cysteine 974 and cysteine 1017
Cysteine 974 and cysteine 976
Cysteine 980 and cysteine 1023
Cysteine 974 and cysteine 985
Cysteine 985 and cysteine 1023
Cysteine 985 and cysteine 1017
Cysteine 1021 and cysteine 1023
Cysteine 426 and cysteine 533
Cysteine 509 and cysteine 536
Cysteine 1115 and cysteine 1168
Cysteine 1017 and cysteine 1021
Cysteine 497 and cysteine 523
Cysteine 509 and cysteine 533
Cysteine 980 and cysteine 1027
Cysteine 533 and cysteine 536
Cysteine 494 and cysteine 497
Cysteine 426 and cysteine 536
Cysteine 923 and cysteine 946
Cysteine 1017 and cysteine 1027
Cysteine 985 and cysteine 994
Cysteine 976 and cysteine 987
Cysteine 985 and cysteine 1021
6mm1 B 426 B 428
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 426 and 428.
Details
Redox score ?
94
PDB code
6mm1
Structure name
structure of the cysteine-rich region from human ehmt2
Structure deposition date
2018-09-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
1
% buried
70
Peptide accession
Q96KQ7
Residue number A
426
Residue number B
428
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 426 of Histone-lysine N-methyltransferase EHMT2
Cysteine 428 of Histone-lysine N-methyltransferase EHMT2
5jiy A 1115 A 1170
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 1115 and 1170.
Details
Redox score ?
92
PDB code
5jiy
Structure name
structure of g9a set-domain with histone h3k9norleucine mutant peptide and bound s-adenosylmethionine
Structure deposition date
2016-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
1
% buried
40
Peptide accession
Q96KQ7
Residue number A
1115
Residue number B
1170
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 1115 of Histone-lysine N-methyltransferase EHMT2
Cysteine 1170 of Histone-lysine N-methyltransferase EHMT2
7btv B 1023 B 1027
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 1023 and 1027.
Details
Redox score ?
87
PDB code
7btv
Structure name
crystal structure of ehmt2 set domain in complex with compound 5
Structure deposition date
2020-04-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
3
% buried
65
Peptide accession
Q96KQ7
Residue number A
1023
Residue number B
1027
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 1023 of Histone-lysine N-methyltransferase EHMT2
Cysteine 1027 of Histone-lysine N-methyltransferase EHMT2
5jj0 A 1115 A 1175
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 1115 and 1175.
Details
Redox score ?
86
PDB code
5jj0
Structure name
structure of g9a set-domain with histone h3k9m peptide and excess sah
Structure deposition date
2016-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
6
% buried
34
Peptide accession
Q96KQ7
Residue number A
1115
Residue number B
1175
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 1115 of Histone-lysine N-methyltransferase EHMT2
Cysteine 1175 of Histone-lysine N-methyltransferase EHMT2
7buc A 1170 A 1175
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 1170 and 1175.
Details
Redox score ?
86
PDB code
7buc
Structure name
crystal structure of ehmt2 set domain in complex with compound 13
Structure deposition date
2020-04-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
6
% buried
26
Peptide accession
Q96KQ7
Residue number A
1170
Residue number B
1175
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 1170 of Histone-lysine N-methyltransferase EHMT2
Cysteine 1175 of Histone-lysine N-methyltransferase EHMT2
6mm1 B 446 B 459
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 446 and 459.
Details
Redox score ?
85
PDB code
6mm1
Structure name
structure of the cysteine-rich region from human ehmt2
Structure deposition date
2018-09-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
5
% buried
30
Peptide accession
Q96KQ7
Residue number A
446
Residue number B
459
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 446 of Histone-lysine N-methyltransferase EHMT2
Cysteine 459 of Histone-lysine N-methyltransferase EHMT2
7btv A 1168 A 1175
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 1168 and 1175.
Details
Redox score ?
85
PDB code
7btv
Structure name
crystal structure of ehmt2 set domain in complex with compound 5
Structure deposition date
2020-04-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
6
% buried
38
Peptide accession
Q96KQ7
Residue number A
1168
Residue number B
1175
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 1168 of Histone-lysine N-methyltransferase EHMT2
Cysteine 1175 of Histone-lysine N-methyltransferase EHMT2
6mm1 A 459 A 481
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 459 and 481.
Details
Redox score ?
83
PDB code
6mm1
Structure name
structure of the cysteine-rich region from human ehmt2
Structure deposition date
2018-09-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
6
% buried
21
Peptide accession
Q96KQ7
Residue number A
459
Residue number B
481
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 459 of Histone-lysine N-methyltransferase EHMT2
Cysteine 481 of Histone-lysine N-methyltransferase EHMT2
5vse B 974 B 1021
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 974 and 1021.
Details
Redox score ?
81
PDB code
5vse
Structure name
structure of human g9a set-domain (ehmt2) in complex with inhibitor 17: n~2~-cyclopentyl-6,7-dimethoxy-n~2~-methyl-n~4~-(1- methylpiperidin-4-yl)quinazoline-2,4-diamine
Structure deposition date
2017-05-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
8
% buried
66
Peptide accession
Q96KQ7
Residue number A
974
Residue number B
1021
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 974 of Histone-lysine N-methyltransferase EHMT2
Cysteine 1021 of Histone-lysine N-methyltransferase EHMT2
5tuy B 1168 B 1170
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 1168 and 1170.
Details
Redox score ?
80
PDB code
5tuy
Structure name
structure of human g9a set-domain (ehmt2) in complex with inhibitor ms0124
Structure deposition date
2016-11-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
8
% buried
42
Peptide accession
Q96KQ7
Residue number A
1168
Residue number B
1170
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 1168 of Histone-lysine N-methyltransferase EHMT2
Cysteine 1170 of Histone-lysine N-methyltransferase EHMT2
3k5k A 976 A 980
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 976 and 980.
Details
Redox score ?
80
PDB code
3k5k
Structure name
discovery of a 2,4-diamino-7-aminoalkoxy-quinazoline as a potent inhibitor of histone lysine methyltransferase, g9a
Structure deposition date
2009-10-07
Thiol separation (Å)
3
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96KQ7
Residue number A
976
Residue number B
980
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 976 of Histone-lysine N-methyltransferase EHMT2
Cysteine 980 of Histone-lysine N-methyltransferase EHMT2
5tuy A 974 A 987
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 974 and 987.
Details
Redox score ?
79
PDB code
5tuy
Structure name
structure of human g9a set-domain (ehmt2) in complex with inhibitor ms0124
Structure deposition date
2016-11-07
Thiol separation (Å)
3
Half-sphere exposure sum ?
71
Minimum pKa ?
8
% buried
60
Peptide accession
Q96KQ7
Residue number A
974
Residue number B
987
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 974 of Histone-lysine N-methyltransferase EHMT2
Cysteine 987 of Histone-lysine N-methyltransferase EHMT2
6mm1 D 446 D 481
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 446 and 481.
Details
Redox score ?
79
PDB code
6mm1
Structure name
structure of the cysteine-rich region from human ehmt2
Structure deposition date
2018-09-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
7
% buried
32
Peptide accession
Q96KQ7
Residue number A
446
Residue number B
481
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 446 of Histone-lysine N-methyltransferase EHMT2
Cysteine 481 of Histone-lysine N-methyltransferase EHMT2
3k5k A 974 A 980
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 974 and 980.
Details
Redox score ?
79
PDB code
3k5k
Structure name
discovery of a 2,4-diamino-7-aminoalkoxy-quinazoline as a potent inhibitor of histone lysine methyltransferase, g9a
Structure deposition date
2009-10-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96KQ7
Residue number A
974
Residue number B
980
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 974 of Histone-lysine N-methyltransferase EHMT2
Cysteine 980 of Histone-lysine N-methyltransferase EHMT2
2o8j A 937 A 946
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 937 and 946.
Details
Redox score ?
78
PDB code
2o8j
Structure name
human euchromatic histone methyltransferase 2
Structure deposition date
2006-12-12
Thiol separation (Å)
3
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
44
Peptide accession
Q96KQ7
Residue number A
937
Residue number B
946
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 937 of Histone-lysine N-methyltransferase EHMT2
Cysteine 946 of Histone-lysine N-methyltransferase EHMT2
7dcf A 987 A 1023
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 987 and 1023.
Details
Redox score ?
78
PDB code
7dcf
Structure name
crystal structure of ehmt2 set domain in complex with compound 10
Structure deposition date
2020-10-26
Thiol separation (Å)
6
Half-sphere exposure sum ?
nan
Minimum pKa ?
2
% buried
53
Peptide accession
Q96KQ7
Residue number A
987
Residue number B
1023
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 987 of Histone-lysine N-methyltransferase EHMT2
Cysteine 1023 of Histone-lysine N-methyltransferase EHMT2
5jin A 974 A 1023
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 974 and 1023.
Details
Redox score ?
77
PDB code
5jin
Structure name
structure of g9a set-domain with histone h3k9m mutant peptide and bound s-adenosylmethionine
Structure deposition date
2016-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
8
% buried
nan
Peptide accession
Q96KQ7
Residue number A
974
Residue number B
1023
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 974 of Histone-lysine N-methyltransferase EHMT2
Cysteine 1023 of Histone-lysine N-methyltransferase EHMT2
7buc B 976 B 985
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 976 and 985.
Details
Redox score ?
77
PDB code
7buc
Structure name
crystal structure of ehmt2 set domain in complex with compound 13
Structure deposition date
2020-04-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
10
% buried
nan
Peptide accession
Q96KQ7
Residue number A
976
Residue number B
985
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 976 of Histone-lysine N-methyltransferase EHMT2
Cysteine 985 of Histone-lysine N-methyltransferase EHMT2
5jin A 974 A 1017
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 974 and 1017.
Details
Redox score ?
77
PDB code
5jin
Structure name
structure of g9a set-domain with histone h3k9m mutant peptide and bound s-adenosylmethionine
Structure deposition date
2016-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
8
% buried
nan
Peptide accession
Q96KQ7
Residue number A
974
Residue number B
1017
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 974 of Histone-lysine N-methyltransferase EHMT2
Cysteine 1017 of Histone-lysine N-methyltransferase EHMT2
7t7l B 974 B 976
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 974 and 976.
Details
Redox score ?
77
PDB code
7t7l
Structure name
structure of human g9a set-domain (ehmt2) in complex with covalent inhibitor (compound 1)
Structure deposition date
2021-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
nan
Peptide accession
Q96KQ7
Residue number A
974
Residue number B
976
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 974 of Histone-lysine N-methyltransferase EHMT2
Cysteine 976 of Histone-lysine N-methyltransferase EHMT2
5v9i D 980 D 1023
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 980 and 1023.
Details
Redox score ?
77
PDB code
5v9i
Structure name
crystal structure of catalytic domain of g9a with ms0105
Structure deposition date
2017-03-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96KQ7
Residue number A
980
Residue number B
1023
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 980 of Histone-lysine N-methyltransferase EHMT2
Cysteine 1023 of Histone-lysine N-methyltransferase EHMT2
3rjw B 974 B 985
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 974 and 985.
Details
Redox score ?
76
PDB code
3rjw
Structure name
crystal structure of histone lysine methyltransferase g9a with an inhibitor
Structure deposition date
2011-04-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96KQ7
Residue number A
974
Residue number B
985
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 974 of Histone-lysine N-methyltransferase EHMT2
Cysteine 985 of Histone-lysine N-methyltransferase EHMT2
4nvq B 985 B 1023
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 985 and 1023.
Details
Redox score ?
76
PDB code
4nvq
Structure name
human g9a in complex with inhibitor a-366
Structure deposition date
2013-12-05
Thiol separation (Å)
7
Half-sphere exposure sum ?
61
Minimum pKa ?
2
% buried
46
Peptide accession
Q96KQ7
Residue number A
985
Residue number B
1023
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 985 of Histone-lysine N-methyltransferase EHMT2
Cysteine 1023 of Histone-lysine N-methyltransferase EHMT2
5vsc B 985 B 1017
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 985 and 1017.
Details
Redox score ?
76
PDB code
5vsc
Structure name
structure of human g9a set-domain (ehmt2) in complex with inhibitor 13
Structure deposition date
2017-05-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
7
% buried
nan
Peptide accession
Q96KQ7
Residue number A
985
Residue number B
1017
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 985 of Histone-lysine N-methyltransferase EHMT2
Cysteine 1017 of Histone-lysine N-methyltransferase EHMT2
7buc B 1021 B 1023
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 1021 and 1023.
Details
Redox score ?
74
PDB code
7buc
Structure name
crystal structure of ehmt2 set domain in complex with compound 13
Structure deposition date
2020-04-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
8
% buried
nan
Peptide accession
Q96KQ7
Residue number A
1021
Residue number B
1023
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 1021 of Histone-lysine N-methyltransferase EHMT2
Cysteine 1023 of Histone-lysine N-methyltransferase EHMT2
6mm1 C 426 C 533
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 426 and 533.
Details
Redox score ?
73
PDB code
6mm1
Structure name
structure of the cysteine-rich region from human ehmt2
Structure deposition date
2018-09-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
76
Minimum pKa ?
0
% buried
63
Peptide accession
Q96KQ7
Residue number A
426
Residue number B
533
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 426 of Histone-lysine N-methyltransferase EHMT2
Cysteine 533 of Histone-lysine N-methyltransferase EHMT2
6mm1 B 509 B 536
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 509 and 536.
Details
Redox score ?
73
PDB code
6mm1
Structure name
structure of the cysteine-rich region from human ehmt2
Structure deposition date
2018-09-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
8
% buried
40
Peptide accession
Q96KQ7
Residue number A
509
Residue number B
536
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 509 of Histone-lysine N-methyltransferase EHMT2
Cysteine 536 of Histone-lysine N-methyltransferase EHMT2
7btv B 1115 B 1168
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 1115 and 1168.
Details
Redox score ?
73
PDB code
7btv
Structure name
crystal structure of ehmt2 set domain in complex with compound 5
Structure deposition date
2020-04-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
11
% buried
43
Peptide accession
Q96KQ7
Residue number A
1115
Residue number B
1168
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 1115 of Histone-lysine N-methyltransferase EHMT2
Cysteine 1168 of Histone-lysine N-methyltransferase EHMT2
5v9i A 1017 A 1021
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 1017 and 1021.
Details
Redox score ?
72
PDB code
5v9i
Structure name
crystal structure of catalytic domain of g9a with ms0105
Structure deposition date
2017-03-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96KQ7
Residue number A
1017
Residue number B
1021
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 1017 of Histone-lysine N-methyltransferase EHMT2
Cysteine 1021 of Histone-lysine N-methyltransferase EHMT2
6mm1 B 497 B 523
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 497 and 523.
Details
Redox score ?
72
PDB code
6mm1
Structure name
structure of the cysteine-rich region from human ehmt2
Structure deposition date
2018-09-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
8
% buried
70
Peptide accession
Q96KQ7
Residue number A
497
Residue number B
523
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 497 of Histone-lysine N-methyltransferase EHMT2
Cysteine 523 of Histone-lysine N-methyltransferase EHMT2
6mm1 C 509 C 533
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 509 and 533.
Details
Redox score ?
71
PDB code
6mm1
Structure name
structure of the cysteine-rich region from human ehmt2
Structure deposition date
2018-09-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
10
% buried
52
Peptide accession
Q96KQ7
Residue number A
509
Residue number B
533
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 509 of Histone-lysine N-methyltransferase EHMT2
Cysteine 533 of Histone-lysine N-methyltransferase EHMT2
5tuy A 980 A 1027
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 980 and 1027.
Details
Redox score ?
71
PDB code
5tuy
Structure name
structure of human g9a set-domain (ehmt2) in complex with inhibitor ms0124
Structure deposition date
2016-11-07
Thiol separation (Å)
3
Half-sphere exposure sum ?
72
Minimum pKa ?
13
% buried
58
Peptide accession
Q96KQ7
Residue number A
980
Residue number B
1027
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 980 of Histone-lysine N-methyltransferase EHMT2
Cysteine 1027 of Histone-lysine N-methyltransferase EHMT2
6mm1 B 533 B 536
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 533 and 536.
Details
Redox score ?
71
PDB code
6mm1
Structure name
structure of the cysteine-rich region from human ehmt2
Structure deposition date
2018-09-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
8
% buried
54
Peptide accession
Q96KQ7
Residue number A
533
Residue number B
536
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 533 of Histone-lysine N-methyltransferase EHMT2
Cysteine 536 of Histone-lysine N-methyltransferase EHMT2
6mm1 B 494 B 497
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 494 and 497.
Details
Redox score ?
70
PDB code
6mm1
Structure name
structure of the cysteine-rich region from human ehmt2
Structure deposition date
2018-09-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
80
Minimum pKa ?
8
% buried
nan
Peptide accession
Q96KQ7
Residue number A
494
Residue number B
497
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 494 of Histone-lysine N-methyltransferase EHMT2
Cysteine 497 of Histone-lysine N-methyltransferase EHMT2
6mm1 C 426 C 536
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 426 and 536.
Details
Redox score ?
69
PDB code
6mm1
Structure name
structure of the cysteine-rich region from human ehmt2
Structure deposition date
2018-09-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
70
Minimum pKa ?
0
% buried
48
Peptide accession
Q96KQ7
Residue number A
426
Residue number B
536
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 426 of Histone-lysine N-methyltransferase EHMT2
Cysteine 536 of Histone-lysine N-methyltransferase EHMT2
5vsc A 923 A 946
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 923 and 946.
Details
Redox score ?
68
PDB code
5vsc
Structure name
structure of human g9a set-domain (ehmt2) in complex with inhibitor 13
Structure deposition date
2017-05-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
12
% buried
50
Peptide accession
Q96KQ7
Residue number A
923
Residue number B
946
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 923 of Histone-lysine N-methyltransferase EHMT2
Cysteine 946 of Histone-lysine N-methyltransferase EHMT2
5tuy B 1017 B 1027
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 1017 and 1027.
Details
Redox score ?
67
PDB code
5tuy
Structure name
structure of human g9a set-domain (ehmt2) in complex with inhibitor ms0124
Structure deposition date
2016-11-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
78
Minimum pKa ?
13
% buried
nan
Peptide accession
Q96KQ7
Residue number A
1017
Residue number B
1027
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 1017 of Histone-lysine N-methyltransferase EHMT2
Cysteine 1027 of Histone-lysine N-methyltransferase EHMT2
4nvq B 985 B 994
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 985 and 994.
Details
Redox score ?
66
PDB code
4nvq
Structure name
human g9a in complex with inhibitor a-366
Structure deposition date
2013-12-05
Thiol separation (Å)
6
Half-sphere exposure sum ?
60
Minimum pKa ?
8
% buried
48
Peptide accession
Q96KQ7
Residue number A
985
Residue number B
994
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 985 of Histone-lysine N-methyltransferase EHMT2
Cysteine 994 of Histone-lysine N-methyltransferase EHMT2
4nvq B 976 B 987
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 976 and 987.
Details
Redox score ?
65
PDB code
4nvq
Structure name
human g9a in complex with inhibitor a-366
Structure deposition date
2013-12-05
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
29
Peptide accession
Q96KQ7
Residue number A
976
Residue number B
987
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 976 of Histone-lysine N-methyltransferase EHMT2
Cysteine 987 of Histone-lysine N-methyltransferase EHMT2
4nvq B 985 B 1021
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT2 between cysteines 985 and 1021.
Details
Redox score ?
65
PDB code
4nvq
Structure name
human g9a in complex with inhibitor a-366
Structure deposition date
2013-12-05
Thiol separation (Å)
6
Half-sphere exposure sum ?
63
Minimum pKa ?
8
% buried
52
Peptide accession
Q96KQ7
Residue number A
985
Residue number B
1021
Peptide name
Histone-lysine N-methyltransferase EHMT2
Ligandability
Cysteine 985 of Histone-lysine N-methyltransferase EHMT2
Cysteine 1021 of Histone-lysine N-methyltransferase EHMT2
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