ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Histone demethylase UTY

Intramolecular
Cysteine 1278 and cysteine 1281
Cysteine 1278 and cysteine 1308
Cysteine 1278 and cysteine 1305
Cysteine 1111 and cysteine 1181
Cysteine 1281 and cysteine 1308
Cysteine 1281 and cysteine 1305
Cysteine 1305 and cysteine 1308
Cysteine 1100 and cysteine 1194
Cysteine 970 and cysteine 1128
Cysteine 907 and cysteine 1100
A redox-regulated disulphide may form within Histone demethylase UTY between cysteines 1278 and 1281.

Details

Redox score ?
87
PDB code
5fy1
Structure name
crystal structure of jmjc domain of human histone demethylase uty in complex with n08619b
Structure deposition date
2016-03-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
5
% buried
26
Peptide accession
O14607
Residue number A
1278
Residue number B
1281
Peptide name
Histone demethylase UTY

Ligandability

Cysteine 1278 of Histone demethylase UTY

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 1281 of Histone demethylase UTY

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 demethylase UTY between cysteines 1278 and 1308.

Details

Redox score ?
87
PDB code
5fy1
Structure name
crystal structure of jmjc domain of human histone demethylase uty in complex with n08619b
Structure deposition date
2016-03-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
5
% buried
21
Peptide accession
O14607
Residue number A
1278
Residue number B
1308
Peptide name
Histone demethylase UTY

Ligandability

Cysteine 1278 of Histone demethylase UTY

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 1308 of Histone demethylase UTY

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 demethylase UTY between cysteines 1278 and 1305 (1199 and 1226 respectively in this structure).

Details

Redox score ?
84
PDB code
5fym
Structure name
crystal structure of jmjc domain of human histone demethylase uty in complex with d-2-hydroxyglutarate
Structure deposition date
2016-03-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
5
% buried
42
Peptide accession
O14607
Residue number A
1278
Residue number B
1305
Peptide name
Histone demethylase UTY

Ligandability

Cysteine 1278 of Histone demethylase UTY

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 1305 of Histone demethylase UTY

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 demethylase UTY between cysteines 1111 and 1181.

Details

Redox score ?
77
PDB code
5fy0
Structure name
crystal structure of jmjc domain of human histone demethylase uty in complex with l-malate
Structure deposition date
2016-03-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
6
% buried
98
Peptide accession
O14607
Residue number A
1111
Residue number B
1181
Peptide name
Histone demethylase UTY

Ligandability

Cysteine 1111 of Histone demethylase UTY

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 1181 of Histone demethylase UTY

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 demethylase UTY between cysteines 1281 and 1308.

Details

Redox score ?
77
PDB code
5fxw
Structure name
crystal structure of jmjc domain of human histone demethylase uty in complex with fumarate
Structure deposition date
2016-03-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
8
% buried
16
Peptide accession
O14607
Residue number A
1281
Residue number B
1308
Peptide name
Histone demethylase UTY

Ligandability

Cysteine 1281 of Histone demethylase UTY

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 1308 of Histone demethylase UTY

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 demethylase UTY between cysteines 1281 and 1305 (1202 and 1226 respectively in this structure).

Details

Redox score ?
75
PDB code
5fy7
Structure name
crystal structure of jmjc domain of human histone demethylase uty in complex with succinate
Structure deposition date
2016-03-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
8
% buried
31
Peptide accession
O14607
Residue number A
1281
Residue number B
1305
Peptide name
Histone demethylase UTY

Ligandability

Cysteine 1281 of Histone demethylase UTY

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 1305 of Histone demethylase UTY

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 demethylase UTY between cysteines 1305 and 1308.

Details

Redox score ?
69
PDB code
4uf0
Structure name
crystal structure of jmjc domain of human histone demethylase uty in complex with epitherapuetic compound 2-(((2-((2-(dimethylamino)ethyl) (ethyl)amino)-2-oxoethyl)amino)methyl)isonicotinic acid
Structure deposition date
2014-12-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
11
% buried
52
Peptide accession
O14607
Residue number A
1305
Residue number B
1308
Peptide name
Histone demethylase UTY

Ligandability

Cysteine 1305 of Histone demethylase UTY

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 1308 of Histone demethylase UTY

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 demethylase UTY between cysteines 1100 and 1194 (1021 and 1115 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
5fy7
Structure name
crystal structure of jmjc domain of human histone demethylase uty in complex with succinate
Structure deposition date
2016-03-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
77
Minimum pKa ?
11
% buried
84
Peptide accession
O14607
Residue number A
1100
Residue number B
1194
Peptide name
Histone demethylase UTY

Ligandability

Cysteine 1100 of Histone demethylase UTY

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 demethylase UTY

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 demethylase UTY between cysteines 970 and 1128 (891 and 1049 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
5fym
Structure name
crystal structure of jmjc domain of human histone demethylase uty in complex with d-2-hydroxyglutarate
Structure deposition date
2016-03-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
11
% buried
79
Peptide accession
O14607
Residue number A
970
Residue number B
1128
Peptide name
Histone demethylase UTY

Ligandability

Cysteine 970 of Histone demethylase UTY

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 1128 of Histone demethylase UTY

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 demethylase UTY between cysteines 907 and 1100. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
5fxz
Structure name
crystal structure of jmjc domain of human histone demethylase uty in complex with citrate
Structure deposition date
2016-03-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
96
Peptide accession
O14607
Residue number A
907
Residue number B
1100
Peptide name
Histone demethylase UTY

Ligandability

Cysteine 907 of Histone demethylase UTY

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 1100 of Histone demethylase UTY

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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