E3 ubiquitin-protein ligase UBR1
Intramolecular
Cysteine 99 and cysteine 127
Cysteine 99 and cysteine 149
Cysteine 99 and cysteine 124
Cysteine 127 and cysteine 163
Cysteine 151 and cysteine 163
Cysteine 99 and cysteine 151
Cysteine 112 and cysteine 115
Cysteine 124 and cysteine 127
Cysteine 127 and cysteine 151
Cysteine 124 and cysteine 149
More...Cysteine 99 and cysteine 163
Cysteine 149 and cysteine 151
Cysteine 127 and cysteine 149
Cysteine 124 and cysteine 163
Cysteine 124 and cysteine 151
Cysteine 149 and cysteine 163
3ny1 A 99 A 127
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR1 between cysteines 99 and 127.
Details
Redox score ?
94
PDB code
3ny1
Structure name
structure of the ubr-box of the ubr1 ubiquitin ligase
Structure deposition date
2010-07-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
0
% buried
42
Peptide accession
Q8IWV7
Residue number A
99
Residue number B
127
Peptide name
E3 ubiquitin-protein ligase UBR1
Ligandability
Cysteine 99 of E3 ubiquitin-protein ligase UBR1
Cysteine 127 of E3 ubiquitin-protein ligase UBR1
3ny1 A 99 A 149
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR1 between cysteines 99 and 149.
Details
Redox score ?
91
PDB code
3ny1
Structure name
structure of the ubr-box of the ubr1 ubiquitin ligase
Structure deposition date
2010-07-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
0
% buried
60
Peptide accession
Q8IWV7
Residue number A
99
Residue number B
149
Peptide name
E3 ubiquitin-protein ligase UBR1
Ligandability
Cysteine 99 of E3 ubiquitin-protein ligase UBR1
Cysteine 149 of E3 ubiquitin-protein ligase UBR1
3ny1 A 99 A 124
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR1 between cysteines 99 and 124.
Details
Redox score ?
89
PDB code
3ny1
Structure name
structure of the ubr-box of the ubr1 ubiquitin ligase
Structure deposition date
2010-07-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
0
% buried
46
Peptide accession
Q8IWV7
Residue number A
99
Residue number B
124
Peptide name
E3 ubiquitin-protein ligase UBR1
Ligandability
Cysteine 99 of E3 ubiquitin-protein ligase UBR1
Cysteine 124 of E3 ubiquitin-protein ligase UBR1
3ny1 A 127 A 163
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR1 between cysteines 127 and 163.
Details
Redox score ?
81
PDB code
3ny1
Structure name
structure of the ubr-box of the ubr1 ubiquitin ligase
Structure deposition date
2010-07-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
7
% buried
32
Peptide accession
Q8IWV7
Residue number A
127
Residue number B
163
Peptide name
E3 ubiquitin-protein ligase UBR1
Ligandability
Cysteine 127 of E3 ubiquitin-protein ligase UBR1
Cysteine 163 of E3 ubiquitin-protein ligase UBR1
5tdc C 151 C 163
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR1 between cysteines 151 and 163.
Details
Redox score ?
80
PDB code
5tdc
Structure name
crystal structure of the human ubr-box domain from ubr1 in complex with monomethylated arginine peptide
Structure deposition date
2016-09-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
7
% buried
28
Peptide accession
Q8IWV7
Residue number A
151
Residue number B
163
Peptide name
E3 ubiquitin-protein ligase UBR1
Ligandability
Cysteine 151 of E3 ubiquitin-protein ligase UBR1
Cysteine 163 of E3 ubiquitin-protein ligase UBR1
3ny1 A 99 A 151
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR1 between cysteines 99 and 151.
Details
Redox score ?
78
PDB code
3ny1
Structure name
structure of the ubr-box of the ubr1 ubiquitin ligase
Structure deposition date
2010-07-14
Thiol separation (Å)
6
Half-sphere exposure sum ?
79
Minimum pKa ?
0
% buried
46
Peptide accession
Q8IWV7
Residue number A
99
Residue number B
151
Peptide name
E3 ubiquitin-protein ligase UBR1
Ligandability
Cysteine 99 of E3 ubiquitin-protein ligase UBR1
Cysteine 151 of E3 ubiquitin-protein ligase UBR1
3ny1 B 112 B 115
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR1 between cysteines 112 and 115.
Details
Redox score ?
77
PDB code
3ny1
Structure name
structure of the ubr-box of the ubr1 ubiquitin ligase
Structure deposition date
2010-07-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
8
% buried
21
Peptide accession
Q8IWV7
Residue number A
112
Residue number B
115
Peptide name
E3 ubiquitin-protein ligase UBR1
Ligandability
Cysteine 112 of E3 ubiquitin-protein ligase UBR1
Cysteine 115 of E3 ubiquitin-protein ligase UBR1
3ny1 B 124 B 127
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR1 between cysteines 124 and 127.
Details
Redox score ?
76
PDB code
3ny1
Structure name
structure of the ubr-box of the ubr1 ubiquitin ligase
Structure deposition date
2010-07-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
8
% buried
37
Peptide accession
Q8IWV7
Residue number A
124
Residue number B
127
Peptide name
E3 ubiquitin-protein ligase UBR1
Ligandability
Cysteine 124 of E3 ubiquitin-protein ligase UBR1
Cysteine 127 of E3 ubiquitin-protein ligase UBR1
5tdc C 127 C 151
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR1 between cysteines 127 and 151.
Details
Redox score ?
74
PDB code
5tdc
Structure name
crystal structure of the human ubr-box domain from ubr1 in complex with monomethylated arginine peptide
Structure deposition date
2016-09-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
9
% buried
38
Peptide accession
Q8IWV7
Residue number A
127
Residue number B
151
Peptide name
E3 ubiquitin-protein ligase UBR1
Ligandability
Cysteine 127 of E3 ubiquitin-protein ligase UBR1
Cysteine 151 of E3 ubiquitin-protein ligase UBR1
3ny1 B 124 B 149
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR1 between cysteines 124 and 149.
Details
Redox score ?
73
PDB code
3ny1
Structure name
structure of the ubr-box of the ubr1 ubiquitin ligase
Structure deposition date
2010-07-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
8
% buried
52
Peptide accession
Q8IWV7
Residue number A
124
Residue number B
149
Peptide name
E3 ubiquitin-protein ligase UBR1
Ligandability
Cysteine 124 of E3 ubiquitin-protein ligase UBR1
Cysteine 149 of E3 ubiquitin-protein ligase UBR1
3ny1 B 99 B 163
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR1 between cysteines 99 and 163.
Details
Redox score ?
68
PDB code
3ny1
Structure name
structure of the ubr-box of the ubr1 ubiquitin ligase
Structure deposition date
2010-07-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
54
Minimum pKa ?
6
% buried
18
Peptide accession
Q8IWV7
Residue number A
99
Residue number B
163
Peptide name
E3 ubiquitin-protein ligase UBR1
Ligandability
Cysteine 99 of E3 ubiquitin-protein ligase UBR1
Cysteine 163 of E3 ubiquitin-protein ligase UBR1
3ny1 B 149 B 151
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR1 between cysteines 149 and 151.
Details
Redox score ?
66
PDB code
3ny1
Structure name
structure of the ubr-box of the ubr1 ubiquitin ligase
Structure deposition date
2010-07-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
79
Minimum pKa ?
9
% buried
46
Peptide accession
Q8IWV7
Residue number A
149
Residue number B
151
Peptide name
E3 ubiquitin-protein ligase UBR1
Ligandability
Cysteine 149 of E3 ubiquitin-protein ligase UBR1
Cysteine 151 of E3 ubiquitin-protein ligase UBR1
3ny1 A 127 A 149
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR1 between cysteines 127 and 149.
Details
Redox score ?
64
PDB code
3ny1
Structure name
structure of the ubr-box of the ubr1 ubiquitin ligase
Structure deposition date
2010-07-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
13
% buried
59
Peptide accession
Q8IWV7
Residue number A
127
Residue number B
149
Peptide name
E3 ubiquitin-protein ligase UBR1
Ligandability
Cysteine 127 of E3 ubiquitin-protein ligase UBR1
Cysteine 149 of E3 ubiquitin-protein ligase UBR1
3ny1 A 124 A 163
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR1 between cysteines 124 and 163. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
3ny1
Structure name
structure of the ubr-box of the ubr1 ubiquitin ligase
Structure deposition date
2010-07-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
66
Minimum pKa ?
7
% buried
36
Peptide accession
Q8IWV7
Residue number A
124
Residue number B
163
Peptide name
E3 ubiquitin-protein ligase UBR1
Ligandability
Cysteine 124 of E3 ubiquitin-protein ligase UBR1
Cysteine 163 of E3 ubiquitin-protein ligase UBR1
5tdc C 124 C 151
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR1 between cysteines 124 and 151. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
5tdc
Structure name
crystal structure of the human ubr-box domain from ubr1 in complex with monomethylated arginine peptide
Structure deposition date
2016-09-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
78
Minimum pKa ?
7
% buried
43
Peptide accession
Q8IWV7
Residue number A
124
Residue number B
151
Peptide name
E3 ubiquitin-protein ligase UBR1
Ligandability
Cysteine 124 of E3 ubiquitin-protein ligase UBR1
Cysteine 151 of E3 ubiquitin-protein ligase UBR1
5tdc A 149 A 163
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UBR1 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 ?
44
PDB code
5tdc
Structure name
crystal structure of the human ubr-box domain from ubr1 in complex with monomethylated arginine peptide
Structure deposition date
2016-09-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
72
Minimum pKa ?
14
% buried
nan
Peptide accession
Q8IWV7
Residue number A
149
Residue number B
163
Peptide name
E3 ubiquitin-protein ligase UBR1
Ligandability
Cysteine 149 of E3 ubiquitin-protein ligase UBR1
Cysteine 163 of E3 ubiquitin-protein ligase UBR1
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