ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Nuclear body protein SP140

Intramolecular
Cysteine 704 and cysteine 716
Cysteine 708 and cysteine 733
Cysteine 704 and cysteine 730
Cysteine 693 and cysteine 716
Cysteine 693 and cysteine 696
Cysteine 705 and cysteine 733
Cysteine 730 and cysteine 733
Cysteine 696 and cysteine 716
Cysteine 716 and cysteine 730
Cysteine 705 and cysteine 708
More...
Cysteine 708 and cysteine 730
Cysteine 708 and cysteine 716
Cysteine 693 and cysteine 772
Cysteine 704 and cysteine 733
Cysteine 693 and cysteine 704
Cysteine 705 and cysteine 716
Cysteine 716 and cysteine 733
Cysteine 705 and cysteine 730
Cysteine 772 and cysteine 773
Cysteine 696 and cysteine 704
Cysteine 704 and cysteine 705
Cysteine 716 and cysteine 772
Cysteine 696 and cysteine 772
Cysteine 704 and cysteine 708
Cysteine 730 and cysteine 772
A redox-regulated disulphide may form within Nuclear body protein SP140 between cysteines 704 and 716 (22 and 34 respectively in this structure).

Details

Redox score ?
85
PDB code
2md7
Structure name
nmr structure of human sp140 phd finger trans conformer
Structure deposition date
2013-09-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q13342
Residue number A
704
Residue number B
716
Peptide name
Nuclear body protein SP140

Ligandability

Cysteine 704 of Nuclear body protein SP140

Cysteine 716 of Nuclear body protein SP140

A redox-regulated disulphide may form within Nuclear body protein SP140 between cysteines 708 and 733.

Details

Redox score ?
83
PDB code
6g8r
Structure name
sp140 phd-bromodomain complex with scfv
Structure deposition date
2018-04-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
5
% buried
56
Peptide accession
Q13342
Residue number A
708
Residue number B
733
Peptide name
Nuclear body protein SP140

Ligandability

Cysteine 708 of Nuclear body protein SP140

Cysteine 733 of Nuclear body protein SP140

A redox-regulated disulphide may form within Nuclear body protein SP140 between cysteines 704 and 730 (22 and 48 respectively in this structure).

Details

Redox score ?
83
PDB code
2md8
Structure name
nmr structure of sp140 phd finger cis conformer
Structure deposition date
2013-09-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
6
% buried
nan
Peptide accession
Q13342
Residue number A
704
Residue number B
730
Peptide name
Nuclear body protein SP140

Ligandability

Cysteine 704 of Nuclear body protein SP140

Cysteine 730 of Nuclear body protein SP140

A redox-regulated disulphide may form within Nuclear body protein SP140 between cysteines 693 and 716.

Details

Redox score ?
82
PDB code
6g8r
Structure name
sp140 phd-bromodomain complex with scfv
Structure deposition date
2018-04-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
6
% buried
38
Peptide accession
Q13342
Residue number A
693
Residue number B
716
Peptide name
Nuclear body protein SP140

Ligandability

Cysteine 693 of Nuclear body protein SP140

Cysteine 716 of Nuclear body protein SP140

A redox-regulated disulphide may form within Nuclear body protein SP140 between cysteines 693 and 696.

Details

Redox score ?
82
PDB code
6g8r
Structure name
sp140 phd-bromodomain complex with scfv
Structure deposition date
2018-04-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
6
% buried
24
Peptide accession
Q13342
Residue number A
693
Residue number B
696
Peptide name
Nuclear body protein SP140

Ligandability

Cysteine 693 of Nuclear body protein SP140

Cysteine 696 of Nuclear body protein SP140

A redox-regulated disulphide may form within Nuclear body protein SP140 between cysteines 705 and 733.

Details

Redox score ?
82
PDB code
6g8r
Structure name
sp140 phd-bromodomain complex with scfv
Structure deposition date
2018-04-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
5
% buried
nan
Peptide accession
Q13342
Residue number A
705
Residue number B
733
Peptide name
Nuclear body protein SP140

Ligandability

Cysteine 705 of Nuclear body protein SP140

Cysteine 733 of Nuclear body protein SP140

A redox-regulated disulphide may form within Nuclear body protein SP140 between cysteines 730 and 733.

Details

Redox score ?
79
PDB code
6g8r
Structure name
sp140 phd-bromodomain complex with scfv
Structure deposition date
2018-04-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
5
% buried
73
Peptide accession
Q13342
Residue number A
730
Residue number B
733
Peptide name
Nuclear body protein SP140

Ligandability

Cysteine 730 of Nuclear body protein SP140

Cysteine 733 of Nuclear body protein SP140

A redox-regulated disulphide may form within Nuclear body protein SP140 between cysteines 696 and 716.

Details

Redox score ?
71
PDB code
6g8r
Structure name
sp140 phd-bromodomain complex with scfv
Structure deposition date
2018-04-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
9
% buried
26
Peptide accession
Q13342
Residue number A
696
Residue number B
716
Peptide name
Nuclear body protein SP140

Ligandability

Cysteine 696 of Nuclear body protein SP140

Cysteine 716 of Nuclear body protein SP140

A redox-regulated disulphide may form within Nuclear body protein SP140 between cysteines 716 and 730 (34 and 48 respectively in this structure).

Details

Redox score ?
71
PDB code
2md8
Structure name
nmr structure of sp140 phd finger cis conformer
Structure deposition date
2013-09-02
Thiol separation (Å)
6
Half-sphere exposure sum ?
64
Minimum pKa ?
6
% buried
nan
Peptide accession
Q13342
Residue number A
716
Residue number B
730
Peptide name
Nuclear body protein SP140

Ligandability

Cysteine 716 of Nuclear body protein SP140

Cysteine 730 of Nuclear body protein SP140

A redox-regulated disulphide may form within Nuclear body protein SP140 between cysteines 705 and 708.

Details

Redox score ?
65
PDB code
6g8r
Structure name
sp140 phd-bromodomain complex with scfv
Structure deposition date
2018-04-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
13
% buried
nan
Peptide accession
Q13342
Residue number A
705
Residue number B
708
Peptide name
Nuclear body protein SP140

Ligandability

Cysteine 705 of Nuclear body protein SP140

Cysteine 708 of Nuclear body protein SP140

A redox-regulated disulphide may form within Nuclear body protein SP140 between cysteines 708 and 730.

Details

Redox score ?
61
PDB code
6g8r
Structure name
sp140 phd-bromodomain complex with scfv
Structure deposition date
2018-04-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
13
% buried
71
Peptide accession
Q13342
Residue number A
708
Residue number B
730
Peptide name
Nuclear body protein SP140

Ligandability

Cysteine 708 of Nuclear body protein SP140

Cysteine 730 of Nuclear body protein SP140

A redox-regulated disulphide may form within Nuclear body protein SP140 between cysteines 708 and 716 (26 and 34 respectively in this structure).

Details

Redox score ?
60
PDB code
2md7
Structure name
nmr structure of human sp140 phd finger trans conformer
Structure deposition date
2013-09-02
Thiol separation (Å)
6
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
nan
Peptide accession
Q13342
Residue number A
708
Residue number B
716
Peptide name
Nuclear body protein SP140

Ligandability

Cysteine 708 of Nuclear body protein SP140

Cysteine 716 of Nuclear body protein SP140

A redox-regulated disulphide may form within Nuclear body protein SP140 between cysteines 693 and 772. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
6g8r
Structure name
sp140 phd-bromodomain complex with scfv
Structure deposition date
2018-04-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
53
Minimum pKa ?
6
% buried
55
Peptide accession
Q13342
Residue number A
693
Residue number B
772
Peptide name
Nuclear body protein SP140

Ligandability

Cysteine 693 of Nuclear body protein SP140

Cysteine 772 of Nuclear body protein SP140

A redox-regulated disulphide may form within Nuclear body protein SP140 between cysteines 704 and 733 (22 and 51 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
2md8
Structure name
nmr structure of sp140 phd finger cis conformer
Structure deposition date
2013-09-02
Thiol separation (Å)
7
Half-sphere exposure sum ?
47
Minimum pKa ?
10
% buried
nan
Peptide accession
Q13342
Residue number A
704
Residue number B
733
Peptide name
Nuclear body protein SP140

Ligandability

Cysteine 704 of Nuclear body protein SP140

Cysteine 733 of Nuclear body protein SP140

A redox-regulated disulphide may form within Nuclear body protein SP140 between cysteines 693 and 704 (11 and 22 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
2md8
Structure name
nmr structure of sp140 phd finger cis conformer
Structure deposition date
2013-09-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
49
Minimum pKa ?
8
% buried
nan
Peptide accession
Q13342
Residue number A
693
Residue number B
704
Peptide name
Nuclear body protein SP140

Ligandability

Cysteine 693 of Nuclear body protein SP140

Cysteine 704 of Nuclear body protein SP140

A redox-regulated disulphide may form within Nuclear body protein SP140 between cysteines 705 and 716 (23 and 34 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
2md8
Structure name
nmr structure of sp140 phd finger cis conformer
Structure deposition date
2013-09-02
Thiol separation (Å)
8
Half-sphere exposure sum ?
54
Minimum pKa ?
11
% buried
nan
Peptide accession
Q13342
Residue number A
705
Residue number B
716
Peptide name
Nuclear body protein SP140

Ligandability

Cysteine 705 of Nuclear body protein SP140

Cysteine 716 of Nuclear body protein SP140

A redox-regulated disulphide may form within Nuclear body protein SP140 between cysteines 716 and 733 (34 and 51 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
2md8
Structure name
nmr structure of sp140 phd finger cis conformer
Structure deposition date
2013-09-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
53
Minimum pKa ?
10
% buried
nan
Peptide accession
Q13342
Residue number A
716
Residue number B
733
Peptide name
Nuclear body protein SP140

Ligandability

Cysteine 716 of Nuclear body protein SP140

Cysteine 733 of Nuclear body protein SP140

A redox-regulated disulphide may form within Nuclear body protein SP140 between cysteines 705 and 730. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
6g8r
Structure name
sp140 phd-bromodomain complex with scfv
Structure deposition date
2018-04-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
22
% buried
nan
Peptide accession
Q13342
Residue number A
705
Residue number B
730
Peptide name
Nuclear body protein SP140

Ligandability

Cysteine 705 of Nuclear body protein SP140

Cysteine 730 of Nuclear body protein SP140

A redox-regulated disulphide may form within Nuclear body protein SP140 between cysteines 772 and 773. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
6g8r
Structure name
sp140 phd-bromodomain complex with scfv
Structure deposition date
2018-04-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
50
Peptide accession
Q13342
Residue number A
772
Residue number B
773
Peptide name
Nuclear body protein SP140

Ligandability

Cysteine 772 of Nuclear body protein SP140

Cysteine 773 of Nuclear body protein SP140

A redox-regulated disulphide may form within Nuclear body protein SP140 between cysteines 696 and 704 (14 and 22 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
2md8
Structure name
nmr structure of sp140 phd finger cis conformer
Structure deposition date
2013-09-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
47
Minimum pKa ?
10
% buried
nan
Peptide accession
Q13342
Residue number A
696
Residue number B
704
Peptide name
Nuclear body protein SP140

Ligandability

Cysteine 696 of Nuclear body protein SP140

Cysteine 704 of Nuclear body protein SP140

A redox-regulated disulphide may form within Nuclear body protein SP140 between cysteines 704 and 705. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
6g8r
Structure name
sp140 phd-bromodomain complex with scfv
Structure deposition date
2018-04-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
10
% buried
nan
Peptide accession
Q13342
Residue number A
704
Residue number B
705
Peptide name
Nuclear body protein SP140

Ligandability

Cysteine 704 of Nuclear body protein SP140

Cysteine 705 of Nuclear body protein SP140

A redox-regulated disulphide may form within Nuclear body protein SP140 between cysteines 716 and 772. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
6g8r
Structure name
sp140 phd-bromodomain complex with scfv
Structure deposition date
2018-04-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
11
% buried
58
Peptide accession
Q13342
Residue number A
716
Residue number B
772
Peptide name
Nuclear body protein SP140

Ligandability

Cysteine 716 of Nuclear body protein SP140

Cysteine 772 of Nuclear body protein SP140

A redox-regulated disulphide may form within Nuclear body protein SP140 between cysteines 696 and 772. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
6g8r
Structure name
sp140 phd-bromodomain complex with scfv
Structure deposition date
2018-04-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
42
Peptide accession
Q13342
Residue number A
696
Residue number B
772
Peptide name
Nuclear body protein SP140

Ligandability

Cysteine 696 of Nuclear body protein SP140

Cysteine 772 of Nuclear body protein SP140

A redox-regulated disulphide may form within Nuclear body protein SP140 between cysteines 704 and 708. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
6g8r
Structure name
sp140 phd-bromodomain complex with scfv
Structure deposition date
2018-04-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
37
Peptide accession
Q13342
Residue number A
704
Residue number B
708
Peptide name
Nuclear body protein SP140

Ligandability

Cysteine 704 of Nuclear body protein SP140

Cysteine 708 of Nuclear body protein SP140

A redox-regulated disulphide may form within Nuclear body protein SP140 between cysteines 730 and 772. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
6g8r
Structure name
sp140 phd-bromodomain complex with scfv
Structure deposition date
2018-04-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
81
Peptide accession
Q13342
Residue number A
730
Residue number B
772
Peptide name
Nuclear body protein SP140

Ligandability

Cysteine 730 of Nuclear body protein SP140

Cysteine 772 of Nuclear body protein SP140

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