ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

GATOR complex protein MIOS

Intramolecular
Cysteine 830 and cysteine 858
Cysteine 775 and cysteine 778
Cysteine 740 and cysteine 775
Cysteine 737 and cysteine 740
Cysteine 830 and cysteine 856
Cysteine 830 and cysteine 854
Cysteine 827 and cysteine 830
Cysteine 830 and cysteine 849
Cysteine 737 and cysteine 778
Cysteine 737 and cysteine 775
More...
Cysteine 849 and cysteine 854
Cysteine 827 and cysteine 858
Cysteine 856 and cysteine 858
Cysteine 740 and cysteine 778
Cysteine 65 and cysteine 116
Cysteine 827 and cysteine 856
Cysteine 854 and cysteine 856
Cysteine 854 and cysteine 858
Cysteine 785 and cysteine 788
Cysteine 849 and cysteine 856
Cysteine 827 and cysteine 854
Cysteine 497 and cysteine 621
Cysteine 849 and cysteine 858
Cysteine 827 and cysteine 849
Cysteine 576 and cysteine 589
A redox-regulated disulphide may form within GATOR complex protein MIOS between cysteines 830 and 858.

Details

Redox score ?
93
PDB code
7uhy
Structure name
human gator2 complex
Structure deposition date
2022-03-27
Thiol separation (Å)
3
Half-sphere exposure sum ?
64
Minimum pKa ?
2
% buried
nan
Peptide accession
Q9NXC5
Residue number A
830
Residue number B
858
Peptide name
GATOR complex protein MIOS

Ligandability

Cysteine 830 of GATOR complex protein MIOS

Cysteine 858 of GATOR complex protein MIOS

A redox-regulated disulphide may form within GATOR complex protein MIOS between cysteines 775 and 778.

Details

Redox score ?
93
PDB code
7uhy
Structure name
human gator2 complex
Structure deposition date
2022-03-27
Thiol separation (Å)
3
Half-sphere exposure sum ?
53
Minimum pKa ?
5
% buried
0
Peptide accession
Q9NXC5
Residue number A
775
Residue number B
778
Peptide name
GATOR complex protein MIOS

Ligandability

Cysteine 775 of GATOR complex protein MIOS

Cysteine 778 of GATOR complex protein MIOS

A redox-regulated disulphide may form within GATOR complex protein MIOS between cysteines 740 and 775.

Details

Redox score ?
89
PDB code
7uhy
Structure name
human gator2 complex
Structure deposition date
2022-03-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
5
% buried
0
Peptide accession
Q9NXC5
Residue number A
740
Residue number B
775
Peptide name
GATOR complex protein MIOS

Ligandability

Cysteine 740 of GATOR complex protein MIOS

Cysteine 775 of GATOR complex protein MIOS

A redox-regulated disulphide may form within GATOR complex protein MIOS between cysteines 737 and 740.

Details

Redox score ?
88
PDB code
7uhy
Structure name
human gator2 complex
Structure deposition date
2022-03-27
Thiol separation (Å)
3
Half-sphere exposure sum ?
48
Minimum pKa ?
7
% buried
6
Peptide accession
Q9NXC5
Residue number A
737
Residue number B
740
Peptide name
GATOR complex protein MIOS

Ligandability

Cysteine 737 of GATOR complex protein MIOS

Cysteine 740 of GATOR complex protein MIOS

A redox-regulated disulphide may form within GATOR complex protein MIOS between cysteines 830 and 856.

Details

Redox score ?
87
PDB code
7uhy
Structure name
human gator2 complex
Structure deposition date
2022-03-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
2
% buried
50
Peptide accession
Q9NXC5
Residue number A
830
Residue number B
856
Peptide name
GATOR complex protein MIOS

Ligandability

Cysteine 830 of GATOR complex protein MIOS

Cysteine 856 of GATOR complex protein MIOS

A redox-regulated disulphide may form within GATOR complex protein MIOS between cysteines 830 and 854.

Details

Redox score ?
87
PDB code
7uhy
Structure name
human gator2 complex
Structure deposition date
2022-03-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
2
% buried
53
Peptide accession
Q9NXC5
Residue number A
830
Residue number B
854
Peptide name
GATOR complex protein MIOS

Ligandability

Cysteine 830 of GATOR complex protein MIOS

Cysteine 854 of GATOR complex protein MIOS

A redox-regulated disulphide may form within GATOR complex protein MIOS between cysteines 827 and 830.

Details

Redox score ?
87
PDB code
7uhy
Structure name
human gator2 complex
Structure deposition date
2022-03-27
Thiol separation (Å)
3
Half-sphere exposure sum ?
82
Minimum pKa ?
2
% buried
nan
Peptide accession
Q9NXC5
Residue number A
827
Residue number B
830
Peptide name
GATOR complex protein MIOS

Ligandability

Cysteine 827 of GATOR complex protein MIOS

Cysteine 830 of GATOR complex protein MIOS

A redox-regulated disulphide may form within GATOR complex protein MIOS between cysteines 830 and 849.

Details

Redox score ?
86
PDB code
7uhy
Structure name
human gator2 complex
Structure deposition date
2022-03-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
2
% buried
72
Peptide accession
Q9NXC5
Residue number A
830
Residue number B
849
Peptide name
GATOR complex protein MIOS

Ligandability

Cysteine 830 of GATOR complex protein MIOS

Cysteine 849 of GATOR complex protein MIOS

A redox-regulated disulphide may form within GATOR complex protein MIOS between cysteines 737 and 778.

Details

Redox score ?
86
PDB code
7uhy
Structure name
human gator2 complex
Structure deposition date
2022-03-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
6
% buried
0
Peptide accession
Q9NXC5
Residue number A
737
Residue number B
778
Peptide name
GATOR complex protein MIOS

Ligandability

Cysteine 737 of GATOR complex protein MIOS

Cysteine 778 of GATOR complex protein MIOS

A redox-regulated disulphide may form within GATOR complex protein MIOS between cysteines 737 and 775.

Details

Redox score ?
83
PDB code
7uhy
Structure name
human gator2 complex
Structure deposition date
2022-03-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
6
% buried
10
Peptide accession
Q9NXC5
Residue number A
737
Residue number B
775
Peptide name
GATOR complex protein MIOS

Ligandability

Cysteine 737 of GATOR complex protein MIOS

Cysteine 775 of GATOR complex protein MIOS

A redox-regulated disulphide may form within GATOR complex protein MIOS between cysteines 849 and 854.

Details

Redox score ?
82
PDB code
7uhy
Structure name
human gator2 complex
Structure deposition date
2022-03-27
Thiol separation (Å)
3
Half-sphere exposure sum ?
66
Minimum pKa ?
8
% buried
54
Peptide accession
Q9NXC5
Residue number A
849
Residue number B
854
Peptide name
GATOR complex protein MIOS

Ligandability

Cysteine 849 of GATOR complex protein MIOS

Cysteine 854 of GATOR complex protein MIOS

A redox-regulated disulphide may form within GATOR complex protein MIOS between cysteines 827 and 858.

Details

Redox score ?
79
PDB code
7uhy
Structure name
human gator2 complex
Structure deposition date
2022-03-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NXC5
Residue number A
827
Residue number B
858
Peptide name
GATOR complex protein MIOS

Ligandability

Cysteine 827 of GATOR complex protein MIOS

Cysteine 858 of GATOR complex protein MIOS

A redox-regulated disulphide may form within GATOR complex protein MIOS between cysteines 856 and 858.

Details

Redox score ?
78
PDB code
7uhy
Structure name
human gator2 complex
Structure deposition date
2022-03-27
Thiol separation (Å)
3
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
nan
Peptide accession
Q9NXC5
Residue number A
856
Residue number B
858
Peptide name
GATOR complex protein MIOS

Ligandability

Cysteine 856 of GATOR complex protein MIOS

Cysteine 858 of GATOR complex protein MIOS

A redox-regulated disulphide may form within GATOR complex protein MIOS between cysteines 740 and 778.

Details

Redox score ?
78
PDB code
7uhy
Structure name
human gator2 complex
Structure deposition date
2022-03-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
9
% buried
0
Peptide accession
Q9NXC5
Residue number A
740
Residue number B
778
Peptide name
GATOR complex protein MIOS

Ligandability

Cysteine 740 of GATOR complex protein MIOS

Cysteine 778 of GATOR complex protein MIOS

A redox-regulated disulphide may form within GATOR complex protein MIOS between cysteines 65 and 116.

Details

Redox score ?
77
PDB code
7uhy
Structure name
human gator2 complex
Structure deposition date
2022-03-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
76
Minimum pKa ?
7
% buried
56
Peptide accession
Q9NXC5
Residue number A
65
Residue number B
116
Peptide name
GATOR complex protein MIOS

Ligandability

Cysteine 65 of GATOR complex protein MIOS

Cysteine 116 of GATOR complex protein MIOS

A redox-regulated disulphide may form within GATOR complex protein MIOS between cysteines 827 and 856.

Details

Redox score ?
74
PDB code
7uhy
Structure name
human gator2 complex
Structure deposition date
2022-03-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
nan
Peptide accession
Q9NXC5
Residue number A
827
Residue number B
856
Peptide name
GATOR complex protein MIOS

Ligandability

Cysteine 827 of GATOR complex protein MIOS

Cysteine 856 of GATOR complex protein MIOS

A redox-regulated disulphide may form within GATOR complex protein MIOS between cysteines 854 and 856.

Details

Redox score ?
71
PDB code
7uhy
Structure name
human gator2 complex
Structure deposition date
2022-03-27
Thiol separation (Å)
6
Half-sphere exposure sum ?
44
Minimum pKa ?
8
% buried
38
Peptide accession
Q9NXC5
Residue number A
854
Residue number B
856
Peptide name
GATOR complex protein MIOS

Ligandability

Cysteine 854 of GATOR complex protein MIOS

Cysteine 856 of GATOR complex protein MIOS

A redox-regulated disulphide may form within GATOR complex protein MIOS between cysteines 854 and 858.

Details

Redox score ?
65
PDB code
7uhy
Structure name
human gator2 complex
Structure deposition date
2022-03-27
Thiol separation (Å)
6
Half-sphere exposure sum ?
62
Minimum pKa ?
8
% buried
nan
Peptide accession
Q9NXC5
Residue number A
854
Residue number B
858
Peptide name
GATOR complex protein MIOS

Ligandability

Cysteine 854 of GATOR complex protein MIOS

Cysteine 858 of GATOR complex protein MIOS

A redox-regulated disulphide may form within GATOR complex protein MIOS between cysteines 785 and 788.

Details

Redox score ?
64
PDB code
7uhy
Structure name
human gator2 complex
Structure deposition date
2022-03-27
Thiol separation (Å)
3
Half-sphere exposure sum ?
74
Minimum pKa ?
15
% buried
nan
Peptide accession
Q9NXC5
Residue number A
785
Residue number B
788
Peptide name
GATOR complex protein MIOS

Ligandability

Cysteine 785 of GATOR complex protein MIOS

Cysteine 788 of GATOR complex protein MIOS

A redox-regulated disulphide may form within GATOR complex protein MIOS between cysteines 849 and 856. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
7uhy
Structure name
human gator2 complex
Structure deposition date
2022-03-27
Thiol separation (Å)
6
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
57
Peptide accession
Q9NXC5
Residue number A
849
Residue number B
856
Peptide name
GATOR complex protein MIOS

Ligandability

Cysteine 849 of GATOR complex protein MIOS

Cysteine 856 of GATOR complex protein MIOS

A redox-regulated disulphide may form within GATOR complex protein MIOS between cysteines 827 and 854. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
7uhy
Structure name
human gator2 complex
Structure deposition date
2022-03-27
Thiol separation (Å)
7
Half-sphere exposure sum ?
67
Minimum pKa ?
8
% buried
nan
Peptide accession
Q9NXC5
Residue number A
827
Residue number B
854
Peptide name
GATOR complex protein MIOS

Ligandability

Cysteine 827 of GATOR complex protein MIOS

Cysteine 854 of GATOR complex protein MIOS

A redox-regulated disulphide may form within GATOR complex protein MIOS between cysteines 497 and 621. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
7uhy
Structure name
human gator2 complex
Structure deposition date
2022-03-27
Thiol separation (Å)
6
Half-sphere exposure sum ?
82
Minimum pKa ?
11
% buried
100
Peptide accession
Q9NXC5
Residue number A
497
Residue number B
621
Peptide name
GATOR complex protein MIOS

Ligandability

Cysteine 497 of GATOR complex protein MIOS

Cysteine 621 of GATOR complex protein MIOS

A redox-regulated disulphide may form within GATOR complex protein MIOS between cysteines 849 and 858. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
7uhy
Structure name
human gator2 complex
Structure deposition date
2022-03-27
Thiol separation (Å)
5
Half-sphere exposure sum ?
75
Minimum pKa ?
15
% buried
nan
Peptide accession
Q9NXC5
Residue number A
849
Residue number B
858
Peptide name
GATOR complex protein MIOS

Ligandability

Cysteine 849 of GATOR complex protein MIOS

Cysteine 858 of GATOR complex protein MIOS

A redox-regulated disulphide may form within GATOR complex protein MIOS between cysteines 827 and 849. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
7uhy
Structure name
human gator2 complex
Structure deposition date
2022-03-27
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
15
% buried
nan
Peptide accession
Q9NXC5
Residue number A
827
Residue number B
849
Peptide name
GATOR complex protein MIOS

Ligandability

Cysteine 827 of GATOR complex protein MIOS

Cysteine 849 of GATOR complex protein MIOS

A redox-regulated disulphide may form within GATOR complex protein MIOS between cysteines 576 and 589. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
7uhy
Structure name
human gator2 complex
Structure deposition date
2022-03-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
35
Peptide accession
Q9NXC5
Residue number A
576
Residue number B
589
Peptide name
GATOR complex protein MIOS

Ligandability

Cysteine 576 of GATOR complex protein MIOS

Cysteine 589 of GATOR complex protein MIOS

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