ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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[histone H3]-trimethyl-L-lysine(27) demethylase

Intramolecular
Cysteine 1199 and cysteine 1202
Cysteine 1199 and cysteine 1229
Cysteine 1199 and cysteine 1226
Cysteine 1032 and cysteine 1102
Cysteine 1202 and cysteine 1229
Cysteine 1202 and cysteine 1226
Cysteine 1226 and cysteine 1229
Cysteine 1021 and cysteine 1115
Cysteine 828 and cysteine 1021
A redox-regulated disulphide may form within [histone H3]-trimethyl-L-lysine(27) demethylase between cysteines 1199 and 1202.

Details

Redox score ?
87
PDB code
5a1l
Structure name
crystal structure of jmjc domain of human histone demethylase uty with s21056a
Structure deposition date
2015-05-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
5
% buried
28
Peptide accession
F4MH27
Residue number A
1199
Residue number B
1202
Peptide name
[histone H3]-trimethyl-L-lysine(27) demethylase

Ligandability

Cysteine 1199 of [histone H3]-trimethyl-L-lysine(27) demethylase

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 1202 of [histone H3]-trimethyl-L-lysine(27) demethylase

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 H3]-trimethyl-L-lysine(27) demethylase between cysteines 1199 and 1229.

Details

Redox score ?
86
PDB code
5a1l
Structure name
crystal structure of jmjc domain of human histone demethylase uty with s21056a
Structure deposition date
2015-05-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
5
% buried
23
Peptide accession
F4MH27
Residue number A
1199
Residue number B
1229
Peptide name
[histone H3]-trimethyl-L-lysine(27) demethylase

Ligandability

Cysteine 1199 of [histone H3]-trimethyl-L-lysine(27) demethylase

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 1229 of [histone H3]-trimethyl-L-lysine(27) demethylase

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 H3]-trimethyl-L-lysine(27) demethylase between cysteines 1199 and 1226.

Details

Redox score ?
84
PDB code
5a1l
Structure name
crystal structure of jmjc domain of human histone demethylase uty with s21056a
Structure deposition date
2015-05-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
5
% buried
38
Peptide accession
F4MH27
Residue number A
1199
Residue number B
1226
Peptide name
[histone H3]-trimethyl-L-lysine(27) demethylase

Ligandability

Cysteine 1199 of [histone H3]-trimethyl-L-lysine(27) demethylase

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 1226 of [histone H3]-trimethyl-L-lysine(27) demethylase

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 H3]-trimethyl-L-lysine(27) demethylase between cysteines 1032 and 1102.

Details

Redox score ?
77
PDB code
5a1l
Structure name
crystal structure of jmjc domain of human histone demethylase uty with s21056a
Structure deposition date
2015-05-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
6
% buried
98
Peptide accession
F4MH27
Residue number A
1032
Residue number B
1102
Peptide name
[histone H3]-trimethyl-L-lysine(27) demethylase

Ligandability

Cysteine 1032 of [histone H3]-trimethyl-L-lysine(27) demethylase

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 1102 of [histone H3]-trimethyl-L-lysine(27) demethylase

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 H3]-trimethyl-L-lysine(27) demethylase between cysteines 1202 and 1229.

Details

Redox score ?
76
PDB code
5a1l
Structure name
crystal structure of jmjc domain of human histone demethylase uty with s21056a
Structure deposition date
2015-05-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
8
% buried
18
Peptide accession
F4MH27
Residue number A
1202
Residue number B
1229
Peptide name
[histone H3]-trimethyl-L-lysine(27) demethylase

Ligandability

Cysteine 1202 of [histone H3]-trimethyl-L-lysine(27) demethylase

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 1229 of [histone H3]-trimethyl-L-lysine(27) demethylase

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 H3]-trimethyl-L-lysine(27) demethylase between cysteines 1202 and 1226.

Details

Redox score ?
75
PDB code
5a1l
Structure name
crystal structure of jmjc domain of human histone demethylase uty with s21056a
Structure deposition date
2015-05-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
8
% buried
33
Peptide accession
F4MH27
Residue number A
1202
Residue number B
1226
Peptide name
[histone H3]-trimethyl-L-lysine(27) demethylase

Ligandability

Cysteine 1202 of [histone H3]-trimethyl-L-lysine(27) demethylase

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 1226 of [histone H3]-trimethyl-L-lysine(27) demethylase

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 H3]-trimethyl-L-lysine(27) demethylase between cysteines 1226 and 1229.

Details

Redox score ?
69
PDB code
5a1l
Structure name
crystal structure of jmjc domain of human histone demethylase uty with s21056a
Structure deposition date
2015-05-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
11
% buried
50
Peptide accession
F4MH27
Residue number A
1226
Residue number B
1229
Peptide name
[histone H3]-trimethyl-L-lysine(27) demethylase

Ligandability

Cysteine 1226 of [histone H3]-trimethyl-L-lysine(27) demethylase

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 1229 of [histone H3]-trimethyl-L-lysine(27) demethylase

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 H3]-trimethyl-L-lysine(27) demethylase between cysteines 1021 and 1115. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
5a1l
Structure name
crystal structure of jmjc domain of human histone demethylase uty with s21056a
Structure deposition date
2015-05-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
82
Peptide accession
F4MH27
Residue number A
1021
Residue number B
1115
Peptide name
[histone H3]-trimethyl-L-lysine(27) demethylase

Ligandability

Cysteine 1021 of [histone H3]-trimethyl-L-lysine(27) demethylase

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 H3]-trimethyl-L-lysine(27) demethylase

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 H3]-trimethyl-L-lysine(27) demethylase between cysteines 828 and 1021. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
5a1l
Structure name
crystal structure of jmjc domain of human histone demethylase uty with s21056a
Structure deposition date
2015-05-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
99
Peptide accession
F4MH27
Residue number A
828
Residue number B
1021
Peptide name
[histone H3]-trimethyl-L-lysine(27) demethylase

Ligandability

Cysteine 828 of [histone H3]-trimethyl-L-lysine(27) demethylase

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 1021 of [histone H3]-trimethyl-L-lysine(27) demethylase

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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