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Histone-lysine N-methyltransferase 2A

Intermolecular
Cysteine 1575 and cysteine 1575
Intramolecular
Cysteine 3959 and cysteine 3964
Cysteine 1158 and cysteine 1161
Cysteine 1158 and cysteine 1194
Cysteine 3909 and cysteine 3959
Cysteine 3909 and cysteine 3964
Cysteine 1155 and cysteine 1158
Cysteine 1167 and cysteine 1170
Cysteine 1161 and cysteine 1194
Cysteine 3957 and cysteine 3959
More...
Cysteine 1588 and cysteine 1624
Cysteine 1170 and cysteine 1173
Cysteine 1588 and cysteine 1591
Cysteine 1170 and cysteine 1189
Cysteine 3957 and cysteine 3964
Cysteine 1569 and cysteine 1572
Cysteine 1569 and cysteine 1599
Cysteine 1173 and cysteine 1189
Cysteine 1155 and cysteine 1194
Cysteine 1167 and cysteine 1189
Cysteine 1591 and cysteine 1624
Cysteine 1588 and cysteine 1621
Cysteine 1155 and cysteine 1161
Cysteine 1621 and cysteine 1624
Cysteine 1167 and cysteine 1173
Cysteine 1591 and cysteine 1621
Cysteine 3909 and cysteine 3957
Cysteine 1572 and cysteine 1599
Cysteine 1188 and cysteine 1189
Cysteine 1170 and cysteine 1188
Cysteine 1161 and cysteine 1188
Cysteine 1569 and cysteine 1575
Cysteine 1158 and cysteine 1188
Cysteine 1569 and cysteine 1621
Cysteine 1572 and cysteine 1575
Cysteine 1188 and cysteine 1194
Cysteine 1173 and cysteine 1188
Cysteine 3845 and cysteine 3913
Cysteine 1167 and cysteine 1188
Cysteine 1569 and cysteine 1591
A redox-regulated disulphide may form between two units of Histone-lysine N-methyltransferase 2A at cysteines 1575 and 1575.

Details

Redox score ?
78
PDB code
3lqj
Structure name
crystal structure of mll1 phd3-bromo complexed with h3(1-9)k4me3 peptide
Structure deposition date
2010-02-09
Thiol separation (Å)
3
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
40
Peptide A name
Histone-lysine N-methyltransferase 2A
Peptide B name
Histone-lysine N-methyltransferase 2A
Peptide A accession
Q03164
Peptide B accession
Q03164
Peptide A residue number
1575
Peptide B residue number
1575

Ligandability

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 2A between cysteines 3959 and 3964.

Details

Redox score ?
94
PDB code
5f5e
Structure name
the crystal structure of mll1 set domain with n3816i/q3867l mutation
Structure deposition date
2015-12-04
Thiol separation (Å)
3
Half-sphere exposure sum ?
49
Minimum pKa ?
5
% buried
6
Peptide accession
Q03164
Residue number A
3959
Residue number B
3964
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 3959 of Histone-lysine N-methyltransferase 2A

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 3964 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1158 and 1161.

Details

Redox score ?
90
PDB code
4nw3
Structure name
crystal structure of mll cxxc domain in complex with a cpg dna
Structure deposition date
2013-12-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
5
% buried
0
Peptide accession
Q03164
Residue number A
1158
Residue number B
1161
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1158 of Histone-lysine N-methyltransferase 2A

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 1161 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1158 and 1194.

Details

Redox score ?
89
PDB code
4nw3
Structure name
crystal structure of mll cxxc domain in complex with a cpg dna
Structure deposition date
2013-12-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
5
% buried
0
Peptide accession
Q03164
Residue number A
1158
Residue number B
1194
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1158 of Histone-lysine N-methyltransferase 2A

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 1194 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 3909 and 3959.

Details

Redox score ?
89
PDB code
5f5e
Structure name
the crystal structure of mll1 set domain with n3816i/q3867l mutation
Structure deposition date
2015-12-04
Thiol separation (Å)
3
Half-sphere exposure sum ?
59
Minimum pKa ?
5
% buried
6
Peptide accession
Q03164
Residue number A
3909
Residue number B
3959
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 3909 of Histone-lysine N-methyltransferase 2A

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 3959 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 3909 and 3964.

Details

Redox score ?
89
PDB code
5f5e
Structure name
the crystal structure of mll1 set domain with n3816i/q3867l mutation
Structure deposition date
2015-12-04
Thiol separation (Å)
3
Half-sphere exposure sum ?
46
Minimum pKa ?
8
% buried
0
Peptide accession
Q03164
Residue number A
3909
Residue number B
3964
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 3909 of Histone-lysine N-methyltransferase 2A

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 3964 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1155 and 1158.

Details

Redox score ?
88
PDB code
4nw3
Structure name
crystal structure of mll cxxc domain in complex with a cpg dna
Structure deposition date
2013-12-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
5
% buried
0
Peptide accession
Q03164
Residue number A
1155
Residue number B
1158
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1155 of Histone-lysine N-methyltransferase 2A

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 1158 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1167 and 1170.

Details

Redox score ?
88
PDB code
4nw3
Structure name
crystal structure of mll cxxc domain in complex with a cpg dna
Structure deposition date
2013-12-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
6
% buried
5
Peptide accession
Q03164
Residue number A
1167
Residue number B
1170
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1167 of Histone-lysine N-methyltransferase 2A

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 1170 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1161 and 1194.

Details

Redox score ?
87
PDB code
4nw3
Structure name
crystal structure of mll cxxc domain in complex with a cpg dna
Structure deposition date
2013-12-05
Thiol separation (Å)
3
Half-sphere exposure sum ?
46
Minimum pKa ?
7
% buried
0
Peptide accession
Q03164
Residue number A
1161
Residue number B
1194
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1161 of Histone-lysine N-methyltransferase 2A

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 1194 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 3957 and 3959 (3958 and 3960 respectively in this structure).

Details

Redox score ?
87
PDB code
7w67
Structure name
the crystal structure of mll1 (n3861i/q3867l/c3882ss)-rbbp5-ash2l in complex with h3k4me0 peptide
Structure deposition date
2021-12-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
6
% buried
34
Peptide accession
Q03164
Residue number A
3957
Residue number B
3959
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 3957 of Histone-lysine N-methyltransferase 2A

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 3959 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1588 and 1624.

Details

Redox score ?
86
PDB code
3lqh
Structure name
crystal structure of mll1 phd3-bromo in the free form
Structure deposition date
2010-02-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
6
% buried
11
Peptide accession
Q03164
Residue number A
1588
Residue number B
1624
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1588 of Histone-lysine N-methyltransferase 2A

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 1624 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1170 and 1173.

Details

Redox score ?
86
PDB code
4nw3
Structure name
crystal structure of mll cxxc domain in complex with a cpg dna
Structure deposition date
2013-12-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
6
% buried
8
Peptide accession
Q03164
Residue number A
1170
Residue number B
1173
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1170 of Histone-lysine N-methyltransferase 2A

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 1173 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1588 and 1591.

Details

Redox score ?
86
PDB code
3lqj
Structure name
crystal structure of mll1 phd3-bromo complexed with h3(1-9)k4me3 peptide
Structure deposition date
2010-02-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
5
% buried
19
Peptide accession
Q03164
Residue number A
1588
Residue number B
1591
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1588 of Histone-lysine N-methyltransferase 2A

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 1591 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1170 and 1189.

Details

Redox score ?
85
PDB code
4nw3
Structure name
crystal structure of mll cxxc domain in complex with a cpg dna
Structure deposition date
2013-12-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
6
% buried
10
Peptide accession
Q03164
Residue number A
1170
Residue number B
1189
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1170 of Histone-lysine N-methyltransferase 2A

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 1189 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 3957 and 3964.

Details

Redox score ?
85
PDB code
2w5z
Structure name
ternary complex of the mixed lineage leukaemia (mll1) set domain with the cofactor product s-adenosylhomocysteine and histone peptide
Structure deposition date
2008-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
8
% buried
14
Peptide accession
Q03164
Residue number A
3957
Residue number B
3964
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 3957 of Histone-lysine N-methyltransferase 2A

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 3964 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1569 and 1572.

Details

Redox score ?
84
PDB code
3lqh
Structure name
crystal structure of mll1 phd3-bromo in the free form
Structure deposition date
2010-02-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
6
% buried
12
Peptide accession
Q03164
Residue number A
1569
Residue number B
1572
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1569 of Histone-lysine N-methyltransferase 2A

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 1572 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1569 and 1599.

Details

Redox score ?
84
PDB code
3lqj
Structure name
crystal structure of mll1 phd3-bromo complexed with h3(1-9)k4me3 peptide
Structure deposition date
2010-02-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
5
% buried
34
Peptide accession
Q03164
Residue number A
1569
Residue number B
1599
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1569 of Histone-lysine N-methyltransferase 2A

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 1599 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1173 and 1189.

Details

Redox score ?
82
PDB code
4nw3
Structure name
crystal structure of mll cxxc domain in complex with a cpg dna
Structure deposition date
2013-12-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
7
% buried
7
Peptide accession
Q03164
Residue number A
1173
Residue number B
1189
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1173 of Histone-lysine N-methyltransferase 2A

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 1189 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1155 and 1194.

Details

Redox score ?
82
PDB code
4nw3
Structure name
crystal structure of mll cxxc domain in complex with a cpg dna
Structure deposition date
2013-12-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
8
% buried
0
Peptide accession
Q03164
Residue number A
1155
Residue number B
1194
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1155 of Histone-lysine N-methyltransferase 2A

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 1194 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1167 and 1189.

Details

Redox score ?
82
PDB code
4nw3
Structure name
crystal structure of mll cxxc domain in complex with a cpg dna
Structure deposition date
2013-12-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
7
% buried
4
Peptide accession
Q03164
Residue number A
1167
Residue number B
1189
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1167 of Histone-lysine N-methyltransferase 2A

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 1189 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1591 and 1624.

Details

Redox score ?
81
PDB code
3lqh
Structure name
crystal structure of mll1 phd3-bromo in the free form
Structure deposition date
2010-02-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
8
% buried
2
Peptide accession
Q03164
Residue number A
1591
Residue number B
1624
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1591 of Histone-lysine N-methyltransferase 2A

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 1624 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1588 and 1621.

Details

Redox score ?
81
PDB code
3lqi
Structure name
crystal structure of mll1 phd3-bromo complexed with h3(1-9)k4me2 peptide
Structure deposition date
2010-02-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
6
% buried
39
Peptide accession
Q03164
Residue number A
1588
Residue number B
1621
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1588 of Histone-lysine N-methyltransferase 2A

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 1621 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1155 and 1161.

Details

Redox score ?
80
PDB code
4nw3
Structure name
crystal structure of mll cxxc domain in complex with a cpg dna
Structure deposition date
2013-12-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
7
% buried
0
Peptide accession
Q03164
Residue number A
1155
Residue number B
1161
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1155 of Histone-lysine N-methyltransferase 2A

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 1161 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1621 and 1624.

Details

Redox score ?
79
PDB code
3lqi
Structure name
crystal structure of mll1 phd3-bromo complexed with h3(1-9)k4me2 peptide
Structure deposition date
2010-02-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
8
% buried
12
Peptide accession
Q03164
Residue number A
1621
Residue number B
1624
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1621 of Histone-lysine N-methyltransferase 2A

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 1624 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1167 and 1173.

Details

Redox score ?
78
PDB code
4nw3
Structure name
crystal structure of mll cxxc domain in complex with a cpg dna
Structure deposition date
2013-12-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
9
% buried
2
Peptide accession
Q03164
Residue number A
1167
Residue number B
1173
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1167 of Histone-lysine N-methyltransferase 2A

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 1173 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1591 and 1621.

Details

Redox score ?
77
PDB code
3lqj
Structure name
crystal structure of mll1 phd3-bromo complexed with h3(1-9)k4me3 peptide
Structure deposition date
2010-02-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
8
% buried
20
Peptide accession
Q03164
Residue number A
1591
Residue number B
1621
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1591 of Histone-lysine N-methyltransferase 2A

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 1621 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 3909 and 3957 (3910 and 3958 respectively in this structure).

Details

Redox score ?
75
PDB code
7w67
Structure name
the crystal structure of mll1 (n3861i/q3867l/c3882ss)-rbbp5-ash2l in complex with h3k4me0 peptide
Structure deposition date
2021-12-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
32
Peptide accession
Q03164
Residue number A
3909
Residue number B
3957
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 3909 of Histone-lysine N-methyltransferase 2A

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 3957 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1572 and 1599.

Details

Redox score ?
72
PDB code
3lqi
Structure name
crystal structure of mll1 phd3-bromo complexed with h3(1-9)k4me2 peptide
Structure deposition date
2010-02-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
9
% buried
70
Peptide accession
Q03164
Residue number A
1572
Residue number B
1599
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1572 of Histone-lysine N-methyltransferase 2A

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 1599 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1188 and 1189.

Details

Redox score ?
66
PDB code
4nw3
Structure name
crystal structure of mll cxxc domain in complex with a cpg dna
Structure deposition date
2013-12-05
Thiol separation (Å)
6
Half-sphere exposure sum ?
51
Minimum pKa ?
7
% buried
31
Peptide accession
Q03164
Residue number A
1188
Residue number B
1189
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1188 of Histone-lysine N-methyltransferase 2A

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 1189 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1170 and 1188. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
4nw3
Structure name
crystal structure of mll cxxc domain in complex with a cpg dna
Structure deposition date
2013-12-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
43
Minimum pKa ?
6
% buried
32
Peptide accession
Q03164
Residue number A
1170
Residue number B
1188
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1170 of Histone-lysine N-methyltransferase 2A

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 1188 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1161 and 1188. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
4nw3
Structure name
crystal structure of mll cxxc domain in complex with a cpg dna
Structure deposition date
2013-12-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
48
Minimum pKa ?
7
% buried
26
Peptide accession
Q03164
Residue number A
1161
Residue number B
1188
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1161 of Histone-lysine N-methyltransferase 2A

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 1188 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1569 and 1575 (8 and 14 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
2kyu
Structure name
the solution structure of the phd3 finger of mll
Structure deposition date
2010-06-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
46
Minimum pKa ?
7
% buried
10
Peptide accession
Q03164
Residue number A
1569
Residue number B
1575
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1569 of Histone-lysine N-methyltransferase 2A

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 1575 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1158 and 1188. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
4nw3
Structure name
crystal structure of mll cxxc domain in complex with a cpg dna
Structure deposition date
2013-12-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
43
Minimum pKa ?
5
% buried
26
Peptide accession
Q03164
Residue number A
1158
Residue number B
1188
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1158 of Histone-lysine N-methyltransferase 2A

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 1188 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1569 and 1621. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
3lqj
Structure name
crystal structure of mll1 phd3-bromo complexed with h3(1-9)k4me3 peptide
Structure deposition date
2010-02-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
5
% buried
35
Peptide accession
Q03164
Residue number A
1569
Residue number B
1621
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1569 of Histone-lysine N-methyltransferase 2A

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 1621 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1572 and 1575. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
3lqj
Structure name
crystal structure of mll1 phd3-bromo complexed with h3(1-9)k4me3 peptide
Structure deposition date
2010-02-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
50
Minimum pKa ?
9
% buried
32
Peptide accession
Q03164
Residue number A
1572
Residue number B
1575
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1572 of Histone-lysine N-methyltransferase 2A

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 1575 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1188 and 1194. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
4nw3
Structure name
crystal structure of mll cxxc domain in complex with a cpg dna
Structure deposition date
2013-12-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
48
Minimum pKa ?
10
% buried
26
Peptide accession
Q03164
Residue number A
1188
Residue number B
1194
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1188 of Histone-lysine N-methyltransferase 2A

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 1194 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1173 and 1188. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
4nw3
Structure name
crystal structure of mll cxxc domain in complex with a cpg dna
Structure deposition date
2013-12-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
53
Minimum pKa ?
11
% buried
29
Peptide accession
Q03164
Residue number A
1173
Residue number B
1188
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1173 of Histone-lysine N-methyltransferase 2A

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 1188 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 3845 and 3913. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
5f5e
Structure name
the crystal structure of mll1 set domain with n3816i/q3867l mutation
Structure deposition date
2015-12-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
10
% buried
58
Peptide accession
Q03164
Residue number A
3845
Residue number B
3913
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 3845 of Histone-lysine N-methyltransferase 2A

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 3913 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1167 and 1188. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
4nw3
Structure name
crystal structure of mll cxxc domain in complex with a cpg dna
Structure deposition date
2013-12-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
26
Peptide accession
Q03164
Residue number A
1167
Residue number B
1188
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1167 of Histone-lysine N-methyltransferase 2A

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 1188 of Histone-lysine N-methyltransferase 2A

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 2A between cysteines 1569 and 1591. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
3lqi
Structure name
crystal structure of mll1 phd3-bromo complexed with h3(1-9)k4me2 peptide
Structure deposition date
2010-02-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
52
Minimum pKa ?
8
% buried
nan
Peptide accession
Q03164
Residue number A
1569
Residue number B
1591
Peptide name
Histone-lysine N-methyltransferase 2A

Ligandability

Cysteine 1569 of Histone-lysine N-methyltransferase 2A

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 1591 of Histone-lysine N-methyltransferase 2A

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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