Protein shisa-3 homolog
Intramolecular
Cysteine 60 and cysteine 78
Cysteine 44 and cysteine 65
Cysteine 28 and cysteine 56
Cysteine 57 and cysteine 66
Cysteine 28 and cysteine 44
Cysteine 28 and cysteine 65
Cysteine 44 and cysteine 56
Cysteine 56 and cysteine 65
Cysteine 56 and cysteine 57
Cysteine 44 and cysteine 57
More...Cysteine 28 and cysteine 57
Cysteine 57 and cysteine 65
Cysteine 56 and cysteine 78
Cysteine 44 and cysteine 66
Cysteine 65 and cysteine 66
Cysteine 56 and cysteine 66
Cysteine 28 and cysteine 66
Cysteine 28 and cysteine 78
Cysteine 56 and cysteine 60
5m0w A 60 A 78
A redox-regulated disulphide may form within Protein shisa-3 homolog between cysteines 60 and 78.
Details
Redox score ?
86
PDB code
5m0w
Structure name
n-terminal domain of mouse shisa 3
Structure deposition date
2016-10-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3UPR0
Residue number A
60
Residue number B
78
Peptide name
Protein shisa-3 homolog
Ligandability
Cysteine 60 of Protein shisa-3 homolog
Cysteine 78 of Protein shisa-3 homolog
5m0w A 44 A 65
A redox-regulated disulphide may form within Protein shisa-3 homolog between cysteines 44 and 65.
Details
Redox score ?
85
PDB code
5m0w
Structure name
n-terminal domain of mouse shisa 3
Structure deposition date
2016-10-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3UPR0
Residue number A
44
Residue number B
65
Peptide name
Protein shisa-3 homolog
Ligandability
Cysteine 44 of Protein shisa-3 homolog
Cysteine 65 of Protein shisa-3 homolog
5m0w A 28 A 56
A redox-regulated disulphide may form within Protein shisa-3 homolog between cysteines 28 and 56.
Details
Redox score ?
83
PDB code
5m0w
Structure name
n-terminal domain of mouse shisa 3
Structure deposition date
2016-10-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3UPR0
Residue number A
28
Residue number B
56
Peptide name
Protein shisa-3 homolog
Ligandability
Cysteine 28 of Protein shisa-3 homolog
Cysteine 56 of Protein shisa-3 homolog
5m0w A 57 A 66
A redox-regulated disulphide may form within Protein shisa-3 homolog between cysteines 57 and 66.
Details
Redox score ?
80
PDB code
5m0w
Structure name
n-terminal domain of mouse shisa 3
Structure deposition date
2016-10-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3UPR0
Residue number A
57
Residue number B
66
Peptide name
Protein shisa-3 homolog
Ligandability
Cysteine 57 of Protein shisa-3 homolog
Cysteine 66 of Protein shisa-3 homolog
5m0w A 28 A 44
A redox-regulated disulphide may form within Protein shisa-3 homolog between cysteines 28 and 44.
Details
Redox score ?
75
PDB code
5m0w
Structure name
n-terminal domain of mouse shisa 3
Structure deposition date
2016-10-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3UPR0
Residue number A
28
Residue number B
44
Peptide name
Protein shisa-3 homolog
Ligandability
Cysteine 28 of Protein shisa-3 homolog
Cysteine 44 of Protein shisa-3 homolog
5m0w A 28 A 65
A redox-regulated disulphide may form within Protein shisa-3 homolog between cysteines 28 and 65.
Details
Redox score ?
69
PDB code
5m0w
Structure name
n-terminal domain of mouse shisa 3
Structure deposition date
2016-10-06
Thiol separation (Å)
5
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3UPR0
Residue number A
28
Residue number B
65
Peptide name
Protein shisa-3 homolog
Ligandability
Cysteine 28 of Protein shisa-3 homolog
Cysteine 65 of Protein shisa-3 homolog
5m0w A 44 A 56
A redox-regulated disulphide may form within Protein shisa-3 homolog between cysteines 44 and 56.
Details
Redox score ?
65
PDB code
5m0w
Structure name
n-terminal domain of mouse shisa 3
Structure deposition date
2016-10-06
Thiol separation (Å)
5
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3UPR0
Residue number A
44
Residue number B
56
Peptide name
Protein shisa-3 homolog
Ligandability
Cysteine 44 of Protein shisa-3 homolog
Cysteine 56 of Protein shisa-3 homolog
5m0w A 56 A 65
A redox-regulated disulphide may form within Protein shisa-3 homolog between cysteines 56 and 65. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
5m0w
Structure name
n-terminal domain of mouse shisa 3
Structure deposition date
2016-10-06
Thiol separation (Å)
6
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3UPR0
Residue number A
56
Residue number B
65
Peptide name
Protein shisa-3 homolog
Ligandability
Cysteine 56 of Protein shisa-3 homolog
Cysteine 65 of Protein shisa-3 homolog
5m0w A 56 A 57
A redox-regulated disulphide may form within Protein shisa-3 homolog between cysteines 56 and 57. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
5m0w
Structure name
n-terminal domain of mouse shisa 3
Structure deposition date
2016-10-06
Thiol separation (Å)
7
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3UPR0
Residue number A
56
Residue number B
57
Peptide name
Protein shisa-3 homolog
Ligandability
Cysteine 56 of Protein shisa-3 homolog
Cysteine 57 of Protein shisa-3 homolog
5m0w A 44 A 57
A redox-regulated disulphide may form within Protein shisa-3 homolog between cysteines 44 and 57. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
5m0w
Structure name
n-terminal domain of mouse shisa 3
Structure deposition date
2016-10-06
Thiol separation (Å)
7
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3UPR0
Residue number A
44
Residue number B
57
Peptide name
Protein shisa-3 homolog
Ligandability
Cysteine 44 of Protein shisa-3 homolog
Cysteine 57 of Protein shisa-3 homolog
5m0w A 28 A 57
A redox-regulated disulphide may form within Protein shisa-3 homolog between cysteines 28 and 57. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
5m0w
Structure name
n-terminal domain of mouse shisa 3
Structure deposition date
2016-10-06
Thiol separation (Å)
7
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3UPR0
Residue number A
28
Residue number B
57
Peptide name
Protein shisa-3 homolog
Ligandability
Cysteine 28 of Protein shisa-3 homolog
Cysteine 57 of Protein shisa-3 homolog
5m0w A 57 A 65
A redox-regulated disulphide may form within Protein shisa-3 homolog between cysteines 57 and 65. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
5m0w
Structure name
n-terminal domain of mouse shisa 3
Structure deposition date
2016-10-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3UPR0
Residue number A
57
Residue number B
65
Peptide name
Protein shisa-3 homolog
Ligandability
Cysteine 57 of Protein shisa-3 homolog
Cysteine 65 of Protein shisa-3 homolog
5m0w A 56 A 78
A redox-regulated disulphide may form within Protein shisa-3 homolog between cysteines 56 and 78. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
5m0w
Structure name
n-terminal domain of mouse shisa 3
Structure deposition date
2016-10-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3UPR0
Residue number A
56
Residue number B
78
Peptide name
Protein shisa-3 homolog
Ligandability
Cysteine 56 of Protein shisa-3 homolog
Cysteine 78 of Protein shisa-3 homolog
5m0w A 44 A 66
A redox-regulated disulphide may form within Protein shisa-3 homolog between cysteines 44 and 66. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
5m0w
Structure name
n-terminal domain of mouse shisa 3
Structure deposition date
2016-10-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3UPR0
Residue number A
44
Residue number B
66
Peptide name
Protein shisa-3 homolog
Ligandability
Cysteine 44 of Protein shisa-3 homolog
Cysteine 66 of Protein shisa-3 homolog
5m0w A 65 A 66
A redox-regulated disulphide may form within Protein shisa-3 homolog between cysteines 65 and 66. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
5m0w
Structure name
n-terminal domain of mouse shisa 3
Structure deposition date
2016-10-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3UPR0
Residue number A
65
Residue number B
66
Peptide name
Protein shisa-3 homolog
Ligandability
Cysteine 65 of Protein shisa-3 homolog
Cysteine 66 of Protein shisa-3 homolog
5m0w A 56 A 66
A redox-regulated disulphide may form within Protein shisa-3 homolog between cysteines 56 and 66. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
5m0w
Structure name
n-terminal domain of mouse shisa 3
Structure deposition date
2016-10-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3UPR0
Residue number A
56
Residue number B
66
Peptide name
Protein shisa-3 homolog
Ligandability
Cysteine 56 of Protein shisa-3 homolog
Cysteine 66 of Protein shisa-3 homolog
5m0w A 28 A 66
A redox-regulated disulphide may form within Protein shisa-3 homolog between cysteines 28 and 66. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
5m0w
Structure name
n-terminal domain of mouse shisa 3
Structure deposition date
2016-10-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3UPR0
Residue number A
28
Residue number B
66
Peptide name
Protein shisa-3 homolog
Ligandability
Cysteine 28 of Protein shisa-3 homolog
Cysteine 66 of Protein shisa-3 homolog
5m0w A 28 A 78
A redox-regulated disulphide may form within Protein shisa-3 homolog between cysteines 28 and 78. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
5m0w
Structure name
n-terminal domain of mouse shisa 3
Structure deposition date
2016-10-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3UPR0
Residue number A
28
Residue number B
78
Peptide name
Protein shisa-3 homolog
Ligandability
Cysteine 28 of Protein shisa-3 homolog
Cysteine 78 of Protein shisa-3 homolog
5m0w A 56 A 60
A redox-regulated disulphide may form within Protein shisa-3 homolog between cysteines 56 and 60. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
5m0w
Structure name
n-terminal domain of mouse shisa 3
Structure deposition date
2016-10-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3UPR0
Residue number A
56
Residue number B
60
Peptide name
Protein shisa-3 homolog
Ligandability
Cysteine 56 of Protein shisa-3 homolog
Cysteine 60 of Protein shisa-3 homolog
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