ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

E3 ubiquitin-protein ligase Praja-1

Intramolecular
Cysteine 613 and cysteine 635
Cysteine 595 and cysteine 598
Cysteine 632 and cysteine 635
Cysteine 595 and cysteine 621
Cysteine 598 and cysteine 621
Cysteine 635 and cysteine 637
Cysteine 613 and cysteine 632
Cysteine 613 and cysteine 637
Cysteine 598 and cysteine 599
Cysteine 632 and cysteine 637
More...
Cysteine 595 and cysteine 599
Cysteine 594 and cysteine 599
Cysteine 594 and cysteine 598
Cysteine 594 and cysteine 595
Cysteine 599 and cysteine 621
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Praja-1 between cysteines 613 and 635 (61 and 83 respectively in this structure).

Details

Redox score ?
84
PDB code
2l0b
Structure name
solution nmr structure of zinc finger domain of e3 ubiquitin-protein ligase praja-1 from homo sapiens, northeast structural genomics consortium (nesg) target hr4710b
Structure deposition date
2010-06-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
7
% buried
15
Peptide accession
Q8NG27
Residue number A
613
Residue number B
635
Peptide name
E3 ubiquitin-protein ligase Praja-1

Ligandability

Cysteine 613 of E3 ubiquitin-protein ligase Praja-1

Cysteine 635 of E3 ubiquitin-protein ligase Praja-1

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Praja-1 between cysteines 595 and 598 (43 and 46 respectively in this structure).

Details

Redox score ?
83
PDB code
2l0b
Structure name
solution nmr structure of zinc finger domain of e3 ubiquitin-protein ligase praja-1 from homo sapiens, northeast structural genomics consortium (nesg) target hr4710b
Structure deposition date
2010-06-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
8
% buried
22
Peptide accession
Q8NG27
Residue number A
595
Residue number B
598
Peptide name
E3 ubiquitin-protein ligase Praja-1

Ligandability

Cysteine 595 of E3 ubiquitin-protein ligase Praja-1

Cysteine 598 of E3 ubiquitin-protein ligase Praja-1

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Praja-1 between cysteines 632 and 635 (80 and 83 respectively in this structure).

Details

Redox score ?
82
PDB code
2l0b
Structure name
solution nmr structure of zinc finger domain of e3 ubiquitin-protein ligase praja-1 from homo sapiens, northeast structural genomics consortium (nesg) target hr4710b
Structure deposition date
2010-06-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
7
% buried
28
Peptide accession
Q8NG27
Residue number A
632
Residue number B
635
Peptide name
E3 ubiquitin-protein ligase Praja-1

Ligandability

Cysteine 632 of E3 ubiquitin-protein ligase Praja-1

Cysteine 635 of E3 ubiquitin-protein ligase Praja-1

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Praja-1 between cysteines 595 and 621 (43 and 69 respectively in this structure).

Details

Redox score ?
79
PDB code
2l0b
Structure name
solution nmr structure of zinc finger domain of e3 ubiquitin-protein ligase praja-1 from homo sapiens, northeast structural genomics consortium (nesg) target hr4710b
Structure deposition date
2010-06-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
8
% buried
36
Peptide accession
Q8NG27
Residue number A
595
Residue number B
621
Peptide name
E3 ubiquitin-protein ligase Praja-1

Ligandability

Cysteine 595 of E3 ubiquitin-protein ligase Praja-1

Cysteine 621 of E3 ubiquitin-protein ligase Praja-1

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Praja-1 between cysteines 598 and 621 (46 and 69 respectively in this structure).

Details

Redox score ?
78
PDB code
2l0b
Structure name
solution nmr structure of zinc finger domain of e3 ubiquitin-protein ligase praja-1 from homo sapiens, northeast structural genomics consortium (nesg) target hr4710b
Structure deposition date
2010-06-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
8
% buried
20
Peptide accession
Q8NG27
Residue number A
598
Residue number B
621
Peptide name
E3 ubiquitin-protein ligase Praja-1

Ligandability

Cysteine 598 of E3 ubiquitin-protein ligase Praja-1

Cysteine 621 of E3 ubiquitin-protein ligase Praja-1

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Praja-1 between cysteines 635 and 637 (83 and 85 respectively in this structure).

Details

Redox score ?
75
PDB code
2l0b
Structure name
solution nmr structure of zinc finger domain of e3 ubiquitin-protein ligase praja-1 from homo sapiens, northeast structural genomics consortium (nesg) target hr4710b
Structure deposition date
2010-06-30
Thiol separation (Å)
5
Half-sphere exposure sum ?
41
Minimum pKa ?
7
% buried
6
Peptide accession
Q8NG27
Residue number A
635
Residue number B
637
Peptide name
E3 ubiquitin-protein ligase Praja-1

Ligandability

Cysteine 635 of E3 ubiquitin-protein ligase Praja-1

Cysteine 637 of E3 ubiquitin-protein ligase Praja-1

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Praja-1 between cysteines 613 and 632 (61 and 80 respectively in this structure).

Details

Redox score ?
75
PDB code
2l0b
Structure name
solution nmr structure of zinc finger domain of e3 ubiquitin-protein ligase praja-1 from homo sapiens, northeast structural genomics consortium (nesg) target hr4710b
Structure deposition date
2010-06-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
32
Peptide accession
Q8NG27
Residue number A
613
Residue number B
632
Peptide name
E3 ubiquitin-protein ligase Praja-1

Ligandability

Cysteine 613 of E3 ubiquitin-protein ligase Praja-1

Cysteine 632 of E3 ubiquitin-protein ligase Praja-1

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Praja-1 between cysteines 613 and 637 (61 and 85 respectively in this structure).

Details

Redox score ?
68
PDB code
2l0b
Structure name
solution nmr structure of zinc finger domain of e3 ubiquitin-protein ligase praja-1 from homo sapiens, northeast structural genomics consortium (nesg) target hr4710b
Structure deposition date
2010-06-30
Thiol separation (Å)
6
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
12
Peptide accession
Q8NG27
Residue number A
613
Residue number B
637
Peptide name
E3 ubiquitin-protein ligase Praja-1

Ligandability

Cysteine 613 of E3 ubiquitin-protein ligase Praja-1

Cysteine 637 of E3 ubiquitin-protein ligase Praja-1

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Praja-1 between cysteines 598 and 599 (46 and 47 respectively in this structure).

Details

Redox score ?
62
PDB code
2l0b
Structure name
solution nmr structure of zinc finger domain of e3 ubiquitin-protein ligase praja-1 from homo sapiens, northeast structural genomics consortium (nesg) target hr4710b
Structure deposition date
2010-06-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
30
Minimum pKa ?
8
% buried
2
Peptide accession
Q8NG27
Residue number A
598
Residue number B
599
Peptide name
E3 ubiquitin-protein ligase Praja-1

Ligandability

Cysteine 598 of E3 ubiquitin-protein ligase Praja-1

Cysteine 599 of E3 ubiquitin-protein ligase Praja-1

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Praja-1 between cysteines 632 and 637 (80 and 85 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
2l0b
Structure name
solution nmr structure of zinc finger domain of e3 ubiquitin-protein ligase praja-1 from homo sapiens, northeast structural genomics consortium (nesg) target hr4710b
Structure deposition date
2010-06-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
24
Peptide accession
Q8NG27
Residue number A
632
Residue number B
637
Peptide name
E3 ubiquitin-protein ligase Praja-1

Ligandability

Cysteine 632 of E3 ubiquitin-protein ligase Praja-1

Cysteine 637 of E3 ubiquitin-protein ligase Praja-1

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Praja-1 between cysteines 595 and 599 (43 and 47 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
2l0b
Structure name
solution nmr structure of zinc finger domain of e3 ubiquitin-protein ligase praja-1 from homo sapiens, northeast structural genomics consortium (nesg) target hr4710b
Structure deposition date
2010-06-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
43
Minimum pKa ?
8
% buried
20
Peptide accession
Q8NG27
Residue number A
595
Residue number B
599
Peptide name
E3 ubiquitin-protein ligase Praja-1

Ligandability

Cysteine 595 of E3 ubiquitin-protein ligase Praja-1

Cysteine 599 of E3 ubiquitin-protein ligase Praja-1

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Praja-1 between cysteines 594 and 599 (42 and 47 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
2l0b
Structure name
solution nmr structure of zinc finger domain of e3 ubiquitin-protein ligase praja-1 from homo sapiens, northeast structural genomics consortium (nesg) target hr4710b
Structure deposition date
2010-06-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
33
Minimum pKa ?
9
% buried
0
Peptide accession
Q8NG27
Residue number A
594
Residue number B
599
Peptide name
E3 ubiquitin-protein ligase Praja-1

Ligandability

Cysteine 594 of E3 ubiquitin-protein ligase Praja-1

Cysteine 599 of E3 ubiquitin-protein ligase Praja-1

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Praja-1 between cysteines 594 and 598 (42 and 46 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
2l0b
Structure name
solution nmr structure of zinc finger domain of e3 ubiquitin-protein ligase praja-1 from homo sapiens, northeast structural genomics consortium (nesg) target hr4710b
Structure deposition date
2010-06-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
38
Minimum pKa ?
8
% buried
2
Peptide accession
Q8NG27
Residue number A
594
Residue number B
598
Peptide name
E3 ubiquitin-protein ligase Praja-1

Ligandability

Cysteine 594 of E3 ubiquitin-protein ligase Praja-1

Cysteine 598 of E3 ubiquitin-protein ligase Praja-1

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Praja-1 between cysteines 594 and 595 (42 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 ?
51
PDB code
2l0b
Structure name
solution nmr structure of zinc finger domain of e3 ubiquitin-protein ligase praja-1 from homo sapiens, northeast structural genomics consortium (nesg) target hr4710b
Structure deposition date
2010-06-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
51
Minimum pKa ?
8
% buried
20
Peptide accession
Q8NG27
Residue number A
594
Residue number B
595
Peptide name
E3 ubiquitin-protein ligase Praja-1

Ligandability

Cysteine 594 of E3 ubiquitin-protein ligase Praja-1

Cysteine 595 of E3 ubiquitin-protein ligase Praja-1

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Praja-1 between cysteines 599 and 621 (47 and 69 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
2l0b
Structure name
solution nmr structure of zinc finger domain of e3 ubiquitin-protein ligase praja-1 from homo sapiens, northeast structural genomics consortium (nesg) target hr4710b
Structure deposition date
2010-06-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
39
Minimum pKa ?
9
% buried
17
Peptide accession
Q8NG27
Residue number A
599
Residue number B
621
Peptide name
E3 ubiquitin-protein ligase Praja-1

Ligandability

Cysteine 599 of E3 ubiquitin-protein ligase Praja-1

Cysteine 621 of E3 ubiquitin-protein ligase Praja-1

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