ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

E3 ubiquitin-protein ligase UBR2

Intramolecular
Cysteine 112 and cysteine 115
Cysteine 124 and cysteine 149
Cysteine 99 and cysteine 124
Cysteine 151 and cysteine 163
Cysteine 127 and cysteine 163
Cysteine 99 and cysteine 127
Cysteine 99 and cysteine 149
Cysteine 149 and cysteine 151
Cysteine 127 and cysteine 151
Cysteine 127 and cysteine 149
More...
Cysteine 99 and cysteine 151
Cysteine 124 and cysteine 163
Cysteine 124 and cysteine 151
Cysteine 99 and cysteine 163
Cysteine 149 and cysteine 163
Cysteine 124 and cysteine 127
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR2 between cysteines 112 and 115.

Details

Redox score ?
89
PDB code
3ny2
Structure name
structure of the ubr-box of ubr2 ubiquitin ligase
Structure deposition date
2010-07-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
2
% buried
46
Peptide accession
Q8IWV8
Residue number A
112
Residue number B
115
Peptide name
E3 ubiquitin-protein ligase UBR2

Ligandability

Cysteine 112 of E3 ubiquitin-protein ligase UBR2

Cysteine 115 of E3 ubiquitin-protein ligase UBR2

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR2 between cysteines 124 and 149.

Details

Redox score ?
87
PDB code
3ny2
Structure name
structure of the ubr-box of ubr2 ubiquitin ligase
Structure deposition date
2010-07-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
2
% buried
64
Peptide accession
Q8IWV8
Residue number A
124
Residue number B
149
Peptide name
E3 ubiquitin-protein ligase UBR2

Ligandability

Cysteine 124 of E3 ubiquitin-protein ligase UBR2

Cysteine 149 of E3 ubiquitin-protein ligase UBR2

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR2 between cysteines 99 and 124.

Details

Redox score ?
84
PDB code
5um3
Structure name
crystal structure of the v122l mutant of human ubr-box domain from ubr2
Structure deposition date
2017-01-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
3
% buried
34
Peptide accession
Q8IWV8
Residue number A
99
Residue number B
124
Peptide name
E3 ubiquitin-protein ligase UBR2

Ligandability

Cysteine 99 of E3 ubiquitin-protein ligase UBR2

Cysteine 124 of E3 ubiquitin-protein ligase UBR2

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR2 between cysteines 151 and 163.

Details

Redox score ?
82
PDB code
3ny2
Structure name
structure of the ubr-box of ubr2 ubiquitin ligase
Structure deposition date
2010-07-14
Thiol separation (Å)
3
Half-sphere exposure sum ?
75
Minimum pKa ?
5
% buried
nan
Peptide accession
Q8IWV8
Residue number A
151
Residue number B
163
Peptide name
E3 ubiquitin-protein ligase UBR2

Ligandability

Cysteine 151 of E3 ubiquitin-protein ligase UBR2

Cysteine 163 of E3 ubiquitin-protein ligase UBR2

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR2 between cysteines 127 and 163.

Details

Redox score ?
80
PDB code
5um3
Structure name
crystal structure of the v122l mutant of human ubr-box domain from ubr2
Structure deposition date
2017-01-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
7
% buried
30
Peptide accession
Q8IWV8
Residue number A
127
Residue number B
163
Peptide name
E3 ubiquitin-protein ligase UBR2

Ligandability

Cysteine 127 of E3 ubiquitin-protein ligase UBR2

Cysteine 163 of E3 ubiquitin-protein ligase UBR2

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR2 between cysteines 99 and 127.

Details

Redox score ?
80
PDB code
3ny2
Structure name
structure of the ubr-box of ubr2 ubiquitin ligase
Structure deposition date
2010-07-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
8
% buried
30
Peptide accession
Q8IWV8
Residue number A
99
Residue number B
127
Peptide name
E3 ubiquitin-protein ligase UBR2

Ligandability

Cysteine 99 of E3 ubiquitin-protein ligase UBR2

Cysteine 127 of E3 ubiquitin-protein ligase UBR2

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR2 between cysteines 99 and 149.

Details

Redox score ?
76
PDB code
3ny2
Structure name
structure of the ubr-box of ubr2 ubiquitin ligase
Structure deposition date
2010-07-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
8
% buried
58
Peptide accession
Q8IWV8
Residue number A
99
Residue number B
149
Peptide name
E3 ubiquitin-protein ligase UBR2

Ligandability

Cysteine 99 of E3 ubiquitin-protein ligase UBR2

Cysteine 149 of E3 ubiquitin-protein ligase UBR2

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR2 between cysteines 149 and 151.

Details

Redox score ?
76
PDB code
5tdd
Structure name
human ubr-box from ubr2 in complex with hifs peptide
Structure deposition date
2016-09-19
Thiol separation (Å)
5
Half-sphere exposure sum ?
81
Minimum pKa ?
4
% buried
57
Peptide accession
Q8IWV8
Residue number A
149
Residue number B
151
Peptide name
E3 ubiquitin-protein ligase UBR2

Ligandability

Cysteine 149 of E3 ubiquitin-protein ligase UBR2

Cysteine 151 of E3 ubiquitin-protein ligase UBR2

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR2 between cysteines 127 and 151.

Details

Redox score ?
75
PDB code
5tdb
Structure name
crystal structure of the human ubr-box domain from ubr2 in complex with asymmetrically double methylated arginine peptide
Structure deposition date
2016-09-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
9
% buried
36
Peptide accession
Q8IWV8
Residue number A
127
Residue number B
151
Peptide name
E3 ubiquitin-protein ligase UBR2

Ligandability

Cysteine 127 of E3 ubiquitin-protein ligase UBR2

Cysteine 151 of E3 ubiquitin-protein ligase UBR2

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR2 between cysteines 127 and 149.

Details

Redox score ?
71
PDB code
3ny2
Structure name
structure of the ubr-box of ubr2 ubiquitin ligase
Structure deposition date
2010-07-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
42
Peptide accession
Q8IWV8
Residue number A
127
Residue number B
149
Peptide name
E3 ubiquitin-protein ligase UBR2

Ligandability

Cysteine 127 of E3 ubiquitin-protein ligase UBR2

Cysteine 149 of E3 ubiquitin-protein ligase UBR2

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR2 between cysteines 99 and 151.

Details

Redox score ?
67
PDB code
3ny2
Structure name
structure of the ubr-box of ubr2 ubiquitin ligase
Structure deposition date
2010-07-14
Thiol separation (Å)
6
Half-sphere exposure sum ?
72
Minimum pKa ?
8
% buried
30
Peptide accession
Q8IWV8
Residue number A
99
Residue number B
151
Peptide name
E3 ubiquitin-protein ligase UBR2

Ligandability

Cysteine 99 of E3 ubiquitin-protein ligase UBR2

Cysteine 151 of E3 ubiquitin-protein ligase UBR2

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR2 between cysteines 124 and 163.

Details

Redox score ?
67
PDB code
5um3
Structure name
crystal structure of the v122l mutant of human ubr-box domain from ubr2
Structure deposition date
2017-01-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
70
Minimum pKa ?
3
% buried
32
Peptide accession
Q8IWV8
Residue number A
124
Residue number B
163
Peptide name
E3 ubiquitin-protein ligase UBR2

Ligandability

Cysteine 124 of E3 ubiquitin-protein ligase UBR2

Cysteine 163 of E3 ubiquitin-protein ligase UBR2

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR2 between cysteines 124 and 151.

Details

Redox score ?
65
PDB code
5um3
Structure name
crystal structure of the v122l mutant of human ubr-box domain from ubr2
Structure deposition date
2017-01-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
83
Minimum pKa ?
3
% buried
43
Peptide accession
Q8IWV8
Residue number A
124
Residue number B
151
Peptide name
E3 ubiquitin-protein ligase UBR2

Ligandability

Cysteine 124 of E3 ubiquitin-protein ligase UBR2

Cysteine 151 of E3 ubiquitin-protein ligase UBR2

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR2 between cysteines 99 and 163.

Details

Redox score ?
60
PDB code
3ny2
Structure name
structure of the ubr-box of ubr2 ubiquitin ligase
Structure deposition date
2010-07-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
64
Minimum pKa ?
8
% buried
nan
Peptide accession
Q8IWV8
Residue number A
99
Residue number B
163
Peptide name
E3 ubiquitin-protein ligase UBR2

Ligandability

Cysteine 99 of E3 ubiquitin-protein ligase UBR2

Cysteine 163 of E3 ubiquitin-protein ligase UBR2

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR2 between cysteines 149 and 163. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
3ny2
Structure name
structure of the ubr-box of ubr2 ubiquitin ligase
Structure deposition date
2010-07-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
65
Minimum pKa ?
7
% buried
45
Peptide accession
Q8IWV8
Residue number A
149
Residue number B
163
Peptide name
E3 ubiquitin-protein ligase UBR2

Ligandability

Cysteine 149 of E3 ubiquitin-protein ligase UBR2

Cysteine 163 of E3 ubiquitin-protein ligase UBR2

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR2 between cysteines 124 and 127. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
3ny2
Structure name
structure of the ubr-box of ubr2 ubiquitin ligase
Structure deposition date
2010-07-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
27
% buried
nan
Peptide accession
Q8IWV8
Residue number A
124
Residue number B
127
Peptide name
E3 ubiquitin-protein ligase UBR2

Ligandability

Cysteine 124 of E3 ubiquitin-protein ligase UBR2

Cysteine 127 of E3 ubiquitin-protein ligase UBR2

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