E3 ubiquitin-protein ligase Hakai
Intramolecular
Cysteine 109 and cysteine 112
Cysteine 109 and cysteine 133
Cysteine 166 and cysteine 172
Cysteine 109 and cysteine 130
Cysteine 125 and cysteine 145
Cysteine 112 and cysteine 133
Cysteine 145 and cysteine 148
Cysteine 112 and cysteine 130
Cysteine 125 and cysteine 148
Cysteine 130 and cysteine 133
More...Cysteine 109 and cysteine 145
Cysteine 109 and cysteine 148
Cysteine 112 and cysteine 145
Cysteine 133 and cysteine 145
3vk6 A 4 A 7
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Hakai between cysteines 109 and 112 (4 and 7 respectively in this structure).
Details
Redox score ?
90
PDB code
3vk6
Structure name
crystal structure of a phosphotyrosine binding domain
Structure deposition date
2011-11-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
6
% buried
3
Peptide accession
Q9JIY2
Residue number A
109
Residue number B
112
Peptide name
E3 ubiquitin-protein ligase Hakai
Ligandability
Cysteine 109 of E3 ubiquitin-protein ligase Hakai
Cysteine 112 of E3 ubiquitin-protein ligase Hakai
3vk6 A 4 A 28
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Hakai between cysteines 109 and 133 (4 and 28 respectively in this structure).
Details
Redox score ?
85
PDB code
3vk6
Structure name
crystal structure of a phosphotyrosine binding domain
Structure deposition date
2011-11-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
6
% buried
6
Peptide accession
Q9JIY2
Residue number A
109
Residue number B
133
Peptide name
E3 ubiquitin-protein ligase Hakai
Ligandability
Cysteine 109 of E3 ubiquitin-protein ligase Hakai
Cysteine 133 of E3 ubiquitin-protein ligase Hakai
2mq1 A 61 A 67
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Hakai between cysteines 166 and 172 (61 and 67 respectively in this structure).
Details
Redox score ?
85
PDB code
2mq1
Structure name
phosphotyrosine binding domain
Structure deposition date
2014-06-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
8
% buried
6
Peptide accession
Q9JIY2
Residue number A
166
Residue number B
172
Peptide name
E3 ubiquitin-protein ligase Hakai
Ligandability
Cysteine 166 of E3 ubiquitin-protein ligase Hakai
Cysteine 172 of E3 ubiquitin-protein ligase Hakai
3vk6 A 4 A 25
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Hakai between cysteines 109 and 130 (4 and 25 respectively in this structure).
Details
Redox score ?
84
PDB code
3vk6
Structure name
crystal structure of a phosphotyrosine binding domain
Structure deposition date
2011-11-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
6
% buried
10
Peptide accession
Q9JIY2
Residue number A
109
Residue number B
130
Peptide name
E3 ubiquitin-protein ligase Hakai
Ligandability
Cysteine 109 of E3 ubiquitin-protein ligase Hakai
Cysteine 130 of E3 ubiquitin-protein ligase Hakai
3vk6 A 20 A 40
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Hakai between cysteines 125 and 145 (20 and 40 respectively in this structure).
Details
Redox score ?
80
PDB code
3vk6
Structure name
crystal structure of a phosphotyrosine binding domain
Structure deposition date
2011-11-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
7
% buried
34
Peptide accession
Q9JIY2
Residue number A
125
Residue number B
145
Peptide name
E3 ubiquitin-protein ligase Hakai
Ligandability
Cysteine 125 of E3 ubiquitin-protein ligase Hakai
Cysteine 145 of E3 ubiquitin-protein ligase Hakai
3vk6 A 7 A 28
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Hakai between cysteines 112 and 133 (7 and 28 respectively in this structure).
Details
Redox score ?
79
PDB code
3vk6
Structure name
crystal structure of a phosphotyrosine binding domain
Structure deposition date
2011-11-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
8
% buried
2
Peptide accession
Q9JIY2
Residue number A
112
Residue number B
133
Peptide name
E3 ubiquitin-protein ligase Hakai
Ligandability
Cysteine 112 of E3 ubiquitin-protein ligase Hakai
Cysteine 133 of E3 ubiquitin-protein ligase Hakai
3vk6 A 40 A 43
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Hakai between cysteines 145 and 148 (40 and 43 respectively in this structure).
Details
Redox score ?
79
PDB code
3vk6
Structure name
crystal structure of a phosphotyrosine binding domain
Structure deposition date
2011-11-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
7
% buried
32
Peptide accession
Q9JIY2
Residue number A
145
Residue number B
148
Peptide name
E3 ubiquitin-protein ligase Hakai
Ligandability
Cysteine 145 of E3 ubiquitin-protein ligase Hakai
Cysteine 148 of E3 ubiquitin-protein ligase Hakai
3vk6 A 7 A 25
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Hakai between cysteines 112 and 130 (7 and 25 respectively in this structure).
Details
Redox score ?
78
PDB code
3vk6
Structure name
crystal structure of a phosphotyrosine binding domain
Structure deposition date
2011-11-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
8
% buried
6
Peptide accession
Q9JIY2
Residue number A
112
Residue number B
130
Peptide name
E3 ubiquitin-protein ligase Hakai
Ligandability
Cysteine 112 of E3 ubiquitin-protein ligase Hakai
Cysteine 130 of E3 ubiquitin-protein ligase Hakai
3vk6 A 20 A 43
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Hakai between cysteines 125 and 148 (20 and 43 respectively in this structure).
Details
Redox score ?
75
PDB code
3vk6
Structure name
crystal structure of a phosphotyrosine binding domain
Structure deposition date
2011-11-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
9
% buried
22
Peptide accession
Q9JIY2
Residue number A
125
Residue number B
148
Peptide name
E3 ubiquitin-protein ligase Hakai
Ligandability
Cysteine 125 of E3 ubiquitin-protein ligase Hakai
Cysteine 148 of E3 ubiquitin-protein ligase Hakai
3vk6 A 25 A 28
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Hakai between cysteines 130 and 133 (25 and 28 respectively in this structure).
Details
Redox score ?
71
PDB code
3vk6
Structure name
crystal structure of a phosphotyrosine binding domain
Structure deposition date
2011-11-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
9
% buried
9
Peptide accession
Q9JIY2
Residue number A
130
Residue number B
133
Peptide name
E3 ubiquitin-protein ligase Hakai
Ligandability
Cysteine 130 of E3 ubiquitin-protein ligase Hakai
Cysteine 133 of E3 ubiquitin-protein ligase Hakai
2mq1 A 4 A 40
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Hakai between cysteines 109 and 145 (4 and 40 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
2mq1
Structure name
phosphotyrosine binding domain
Structure deposition date
2014-06-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
6
% buried
32
Peptide accession
Q9JIY2
Residue number A
109
Residue number B
145
Peptide name
E3 ubiquitin-protein ligase Hakai
Ligandability
Cysteine 109 of E3 ubiquitin-protein ligase Hakai
Cysteine 145 of E3 ubiquitin-protein ligase Hakai
2mq1 A 4 A 43
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Hakai between cysteines 109 and 148 (4 and 43 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
2mq1
Structure name
phosphotyrosine binding domain
Structure deposition date
2014-06-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
48
Minimum pKa ?
6
% buried
22
Peptide accession
Q9JIY2
Residue number A
109
Residue number B
148
Peptide name
E3 ubiquitin-protein ligase Hakai
Ligandability
Cysteine 109 of E3 ubiquitin-protein ligase Hakai
Cysteine 148 of E3 ubiquitin-protein ligase Hakai
2mq1 A 7 A 40
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Hakai between cysteines 112 and 145 (7 and 40 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
2mq1
Structure name
phosphotyrosine binding domain
Structure deposition date
2014-06-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
26
Peptide accession
Q9JIY2
Residue number A
112
Residue number B
145
Peptide name
E3 ubiquitin-protein ligase Hakai
Ligandability
Cysteine 112 of E3 ubiquitin-protein ligase Hakai
Cysteine 145 of E3 ubiquitin-protein ligase Hakai
2mq1 A 28 A 40
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Hakai between cysteines 133 and 145 (28 and 40 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
2mq1
Structure name
phosphotyrosine binding domain
Structure deposition date
2014-06-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
9
% buried
32
Peptide accession
Q9JIY2
Residue number A
133
Residue number B
145
Peptide name
E3 ubiquitin-protein ligase Hakai
Ligandability
Cysteine 133 of E3 ubiquitin-protein ligase Hakai
Cysteine 145 of E3 ubiquitin-protein ligase Hakai
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