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Histone-lysine N-methyltransferase EHMT1

Intramolecular
Cysteine 1062 and cysteine 1111
Cysteine 1203 and cysteine 1263
Cysteine 1256 and cysteine 1263
Cysteine 1062 and cysteine 1068
Cysteine 1111 and cysteine 1115
Cysteine 1256 and cysteine 1258
Cysteine 1025 and cysteine 1034
Cysteine 1109 and cysteine 1111
Cysteine 1258 and cysteine 1263
Cysteine 1068 and cysteine 1073
More...
Cysteine 1203 and cysteine 1258
Cysteine 1064 and cysteine 1068
Cysteine 1062 and cysteine 1064
Cysteine 1064 and cysteine 1073
Cysteine 1203 and cysteine 1256
Cysteine 1073 and cysteine 1105
Cysteine 1105 and cysteine 1111
Cysteine 1075 and cysteine 1109
Cysteine 1073 and cysteine 1111
Cysteine 1062 and cysteine 1105
Cysteine 1075 and cysteine 1111
Cysteine 1062 and cysteine 1073
Cysteine 1064 and cysteine 1115
Cysteine 1068 and cysteine 1115
Cysteine 1105 and cysteine 1115
Cysteine 1062 and cysteine 1115
Cysteine 1062 and cysteine 1109
Cysteine 1064 and cysteine 1111
Cysteine 1073 and cysteine 1115
Cysteine 1064 and cysteine 1105
Cysteine 1064 and cysteine 1109
Cysteine 1064 and cysteine 1075
Cysteine 1073 and cysteine 1082
Cysteine 1068 and cysteine 1075
Cysteine 1068 and cysteine 1082
Cysteine 1082 and cysteine 1105
Cysteine 918 and cysteine 954
Cysteine 909 and cysteine 930
Cysteine 1109 and cysteine 1115
Cysteine 1082 and cysteine 1115
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1062 and 1111 (1031 and 1080 respectively in this structure).

Details

Redox score ?
91
PDB code
3sw9
Structure name
glp (g9a-like protein) set domain in complex with dnmt3ak44me0 peptide
Structure deposition date
2011-07-13
Thiol separation (Å)
3
Half-sphere exposure sum ?
65
Minimum pKa ?
4
% buried
nan
Peptide accession
Q9H9B1
Residue number A
1062
Residue number B
1111
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1062 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1111 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1203 and 1263 (1172 and 1232 respectively in this structure).

Details

Redox score ?
88
PDB code
6mbp
Structure name
glp methyltransferase with inhibitor eml741- p3121 crystal form
Structure deposition date
2018-08-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
6
% buried
15
Peptide accession
Q9H9B1
Residue number A
1203
Residue number B
1263
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1203 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1263 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1256 and 1263 (1225 and 1232 respectively in this structure).

Details

Redox score ?
87
PDB code
3mo2
Structure name
human g9a-like (glp, also known as ehmt1) in complex with inhibitor e67
Structure deposition date
2010-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
8
% buried
11
Peptide accession
Q9H9B1
Residue number A
1256
Residue number B
1263
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1256 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1263 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1062 and 1068.

Details

Redox score ?
86
PDB code
7t7m
Structure name
structure of human glp set-domain (ehmt1) in complex with covalent inhibitor (compound 1)
Structure deposition date
2021-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
6
% buried
36
Peptide accession
Q9H9B1
Residue number A
1062
Residue number B
1068
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1062 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1068 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1111 and 1115 (1080 and 1084 respectively in this structure).

Details

Redox score ?
85
PDB code
3mo5
Structure name
human g9a-like (glp, also known as ehmt1) in complex with inhibitor e72
Structure deposition date
2010-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
4
% buried
nan
Peptide accession
Q9H9B1
Residue number A
1111
Residue number B
1115
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1111 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1115 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1256 and 1258.

Details

Redox score ?
84
PDB code
7t7m
Structure name
structure of human glp set-domain (ehmt1) in complex with covalent inhibitor (compound 1)
Structure deposition date
2021-12-15
Thiol separation (Å)
3
Half-sphere exposure sum ?
63
Minimum pKa ?
6
% buried
48
Peptide accession
Q9H9B1
Residue number A
1256
Residue number B
1258
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1256 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1258 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1025 and 1034 (994 and 1003 respectively in this structure).

Details

Redox score ?
83
PDB code
3mo5
Structure name
human g9a-like (glp, also known as ehmt1) in complex with inhibitor e72
Structure deposition date
2010-04-22
Thiol separation (Å)
3
Half-sphere exposure sum ?
61
Minimum pKa ?
8
% buried
54
Peptide accession
Q9H9B1
Residue number A
1025
Residue number B
1034
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1025 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1034 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1109 and 1111 (1078 and 1080 respectively in this structure).

Details

Redox score ?
83
PDB code
3fpd
Structure name
g9a-like protein lysine methyltransferase inhibition by bix- 01294
Structure deposition date
2009-01-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
3
% buried
72
Peptide accession
Q9H9B1
Residue number A
1109
Residue number B
1111
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1109 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1111 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1258 and 1263 (1227 and 1232 respectively in this structure).

Details

Redox score ?
83
PDB code
3fpd
Structure name
g9a-like protein lysine methyltransferase inhibition by bix- 01294
Structure deposition date
2009-01-05
Thiol separation (Å)
5
Half-sphere exposure sum ?
46
Minimum pKa ?
6
% buried
16
Peptide accession
Q9H9B1
Residue number A
1258
Residue number B
1263
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1258 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1263 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1068 and 1073.

Details

Redox score ?
81
PDB code
7t7m
Structure name
structure of human glp set-domain (ehmt1) in complex with covalent inhibitor (compound 1)
Structure deposition date
2021-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
8
% buried
42
Peptide accession
Q9H9B1
Residue number A
1068
Residue number B
1073
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1068 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1073 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1203 and 1258.

Details

Redox score ?
80
PDB code
7t7m
Structure name
structure of human glp set-domain (ehmt1) in complex with covalent inhibitor (compound 1)
Structure deposition date
2021-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
4
% buried
nan
Peptide accession
Q9H9B1
Residue number A
1203
Residue number B
1258
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1203 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1258 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1064 and 1068.

Details

Redox score ?
79
PDB code
7t7m
Structure name
structure of human glp set-domain (ehmt1) in complex with covalent inhibitor (compound 1)
Structure deposition date
2021-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
26
Peptide accession
Q9H9B1
Residue number A
1064
Residue number B
1068
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1064 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1068 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1062 and 1064.

Details

Redox score ?
78
PDB code
7t7m
Structure name
structure of human glp set-domain (ehmt1) in complex with covalent inhibitor (compound 1)
Structure deposition date
2021-12-15
Thiol separation (Å)
3
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
nan
Peptide accession
Q9H9B1
Residue number A
1062
Residue number B
1064
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1062 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1064 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1064 and 1073 (1033 and 1042 respectively in this structure).

Details

Redox score ?
76
PDB code
3mo5
Structure name
human g9a-like (glp, also known as ehmt1) in complex with inhibitor e72
Structure deposition date
2010-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
nan
Peptide accession
Q9H9B1
Residue number A
1064
Residue number B
1073
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1064 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1073 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1203 and 1256 (1172 and 1225 respectively in this structure).

Details

Redox score ?
75
PDB code
6mbp
Structure name
glp methyltransferase with inhibitor eml741- p3121 crystal form
Structure deposition date
2018-08-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
32
Peptide accession
Q9H9B1
Residue number A
1203
Residue number B
1256
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1203 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1256 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1073 and 1105 (1042 and 1074 respectively in this structure).

Details

Redox score ?
75
PDB code
3mo2
Structure name
human g9a-like (glp, also known as ehmt1) in complex with inhibitor e67
Structure deposition date
2010-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
7
% buried
nan
Peptide accession
Q9H9B1
Residue number A
1073
Residue number B
1105
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1073 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1105 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1105 and 1111 (1074 and 1080 respectively in this structure).

Details

Redox score ?
75
PDB code
3mo0
Structure name
human g9a-like (glp, also known as ehmt1) in complex with inhibitor e11
Structure deposition date
2010-04-22
Thiol separation (Å)
3
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H9B1
Residue number A
1105
Residue number B
1111
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1105 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1111 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1075 and 1109.

Details

Redox score ?
74
PDB code
5ttg
Structure name
crystal structure of catalytic domain of glp with ms012
Structure deposition date
2016-11-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H9B1
Residue number A
1075
Residue number B
1109
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1075 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1109 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1073 and 1111 (1042 and 1080 respectively in this structure).

Details

Redox score ?
74
PDB code
3sw9
Structure name
glp (g9a-like protein) set domain in complex with dnmt3ak44me0 peptide
Structure deposition date
2011-07-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
65
Minimum pKa ?
4
% buried
58
Peptide accession
Q9H9B1
Residue number A
1073
Residue number B
1111
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1073 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1111 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1062 and 1105 (1031 and 1074 respectively in this structure).

Details

Redox score ?
73
PDB code
4i51
Structure name
methyltransferase domain of human euchromatic histone methyltransferase 1, mutant y1211a
Structure deposition date
2012-11-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H9B1
Residue number A
1062
Residue number B
1105
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1062 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1105 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1075 and 1111 (1044 and 1080 respectively in this structure).

Details

Redox score ?
71
PDB code
3sw9
Structure name
glp (g9a-like protein) set domain in complex with dnmt3ak44me0 peptide
Structure deposition date
2011-07-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
75
Minimum pKa ?
4
% buried
64
Peptide accession
Q9H9B1
Residue number A
1075
Residue number B
1111
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1075 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1111 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1062 and 1073 (1031 and 1042 respectively in this structure).

Details

Redox score ?
70
PDB code
6mbo
Structure name
glp methyltransferase with inhibitor eml741-p212121 crystal form
Structure deposition date
2018-08-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
12
% buried
nan
Peptide accession
Q9H9B1
Residue number A
1062
Residue number B
1073
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1062 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1073 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1064 and 1115.

Details

Redox score ?
69
PDB code
7t7m
Structure name
structure of human glp set-domain (ehmt1) in complex with covalent inhibitor (compound 1)
Structure deposition date
2021-12-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
57
Minimum pKa ?
3
% buried
31
Peptide accession
Q9H9B1
Residue number A
1064
Residue number B
1115
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1064 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1115 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1068 and 1115 (1037 and 1084 respectively in this structure).

Details

Redox score ?
67
PDB code
3fpd
Structure name
g9a-like protein lysine methyltransferase inhibition by bix- 01294
Structure deposition date
2009-01-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
13
% buried
60
Peptide accession
Q9H9B1
Residue number A
1068
Residue number B
1115
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1068 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1115 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1105 and 1115 (1074 and 1084 respectively in this structure).

Details

Redox score ?
65
PDB code
3sw9
Structure name
glp (g9a-like protein) set domain in complex with dnmt3ak44me0 peptide
Structure deposition date
2011-07-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
13
% buried
nan
Peptide accession
Q9H9B1
Residue number A
1105
Residue number B
1115
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1105 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1115 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1062 and 1115.

Details

Redox score ?
63
PDB code
7t7m
Structure name
structure of human glp set-domain (ehmt1) in complex with covalent inhibitor (compound 1)
Structure deposition date
2021-12-15
Thiol separation (Å)
6
Half-sphere exposure sum ?
71
Minimum pKa ?
8
% buried
68
Peptide accession
Q9H9B1
Residue number A
1062
Residue number B
1115
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1062 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1115 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1062 and 1109 (1031 and 1078 respectively in this structure).

Details

Redox score ?
63
PDB code
3sw9
Structure name
glp (g9a-like protein) set domain in complex with dnmt3ak44me0 peptide
Structure deposition date
2011-07-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
16
% buried
nan
Peptide accession
Q9H9B1
Residue number A
1062
Residue number B
1109
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1062 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1109 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1064 and 1111.

Details

Redox score ?
62
PDB code
7t7m
Structure name
structure of human glp set-domain (ehmt1) in complex with covalent inhibitor (compound 1)
Structure deposition date
2021-12-15
Thiol separation (Å)
6
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
nan
Peptide accession
Q9H9B1
Residue number A
1064
Residue number B
1111
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1064 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1111 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1073 and 1115 (1042 and 1084 respectively in this structure).

Details

Redox score ?
62
PDB code
3mo5
Structure name
human g9a-like (glp, also known as ehmt1) in complex with inhibitor e72
Structure deposition date
2010-04-22
Thiol separation (Å)
7
Half-sphere exposure sum ?
67
Minimum pKa ?
8
% buried
60
Peptide accession
Q9H9B1
Residue number A
1073
Residue number B
1115
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1073 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1115 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1064 and 1105. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
7t7m
Structure name
structure of human glp set-domain (ehmt1) in complex with covalent inhibitor (compound 1)
Structure deposition date
2021-12-15
Thiol separation (Å)
6
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
nan
Peptide accession
Q9H9B1
Residue number A
1064
Residue number B
1105
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1064 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1105 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1064 and 1109 (1033 and 1078 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
3sw9
Structure name
glp (g9a-like protein) set domain in complex with dnmt3ak44me0 peptide
Structure deposition date
2011-07-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
8
% buried
50
Peptide accession
Q9H9B1
Residue number A
1064
Residue number B
1109
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1064 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1109 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1064 and 1075. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
5tuz
Structure name
structure of human glp set-domain (ehmt1) in complex with inhibitor ms0124
Structure deposition date
2016-11-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
65
Minimum pKa ?
10
% buried
46
Peptide accession
Q9H9B1
Residue number A
1064
Residue number B
1075
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1064 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1075 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1073 and 1082 (1042 and 1051 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
2igq
Structure name
human euchromatic histone methyltransferase 1
Structure deposition date
2006-09-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
nan
Peptide accession
Q9H9B1
Residue number A
1073
Residue number B
1082
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1073 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1082 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1068 and 1075. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
7t7m
Structure name
structure of human glp set-domain (ehmt1) in complex with covalent inhibitor (compound 1)
Structure deposition date
2021-12-15
Thiol separation (Å)
6
Half-sphere exposure sum ?
75
Minimum pKa ?
13
% buried
50
Peptide accession
Q9H9B1
Residue number A
1068
Residue number B
1075
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1068 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1075 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1068 and 1082 (1037 and 1051 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
3mo2
Structure name
human g9a-like (glp, also known as ehmt1) in complex with inhibitor e67
Structure deposition date
2010-04-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
70
Minimum pKa ?
10
% buried
58
Peptide accession
Q9H9B1
Residue number A
1068
Residue number B
1082
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1068 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1082 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1082 and 1105. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
5v9j
Structure name
crystal structure of catalytic domain of glp with ms0105
Structure deposition date
2017-03-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H9B1
Residue number A
1082
Residue number B
1105
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1082 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1105 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 918 and 954 (887 and 923 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
3b7b
Structure name
euhmt1 (glp) ankyrin repeat domain (structure 1)
Structure deposition date
2007-10-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
52
Peptide accession
Q9H9B1
Residue number A
918
Residue number B
954
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 918 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 954 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 909 and 930. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
6by9
Structure name
crystal structure of ehmt1
Structure deposition date
2017-12-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H9B1
Residue number A
909
Residue number B
930
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 909 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 930 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1109 and 1115 (1078 and 1084 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
3swc
Structure name
glp (g9a-like protein) set domain in complex with dnmt3ak44me2 peptide
Structure deposition date
2011-07-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
73
Minimum pKa ?
13
% buried
75
Peptide accession
Q9H9B1
Residue number A
1109
Residue number B
1115
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1109 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1115 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EHMT1 between cysteines 1082 and 1115. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
5vsd
Structure name
structure of human glp set-domain (ehmt1) in complex with inhibitor 13
Structure deposition date
2017-05-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
75
Peptide accession
Q9H9B1
Residue number A
1082
Residue number B
1115
Peptide name
Histone-lysine N-methyltransferase EHMT1

Ligandability

Cysteine 1082 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1115 of Histone-lysine N-methyltransferase EHMT1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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