ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

CD160 antigen

Intramolecular
Cysteine 61 and cysteine 68
Cysteine 44 and cysteine 112
Cysteine 68 and cysteine 113
Cysteine 61 and cysteine 113
Cysteine 68 and cysteine 112
Cysteine 44 and cysteine 68
Cysteine 112 and cysteine 113
Cysteine 44 and cysteine 113
Cysteine 44 and cysteine 61
Cysteine 61 and cysteine 112
A redox-regulated disulphide may form within CD160 antigen between cysteines 61 and 68.

Details

Redox score ?
84
PDB code
6ng9
Structure name
crystal structure of human cd160
Structure deposition date
2018-12-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95971
Residue number A
61
Residue number B
68
Peptide name
CD160 antigen

Ligandability

Cysteine 61 of CD160 antigen

Cysteine 68 of CD160 antigen

A redox-regulated disulphide may form within CD160 antigen between cysteines 44 and 112.

Details

Redox score ?
78
PDB code
6ngg
Structure name
crystal structure of human cd160 v58m mutant
Structure deposition date
2018-12-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
93
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95971
Residue number A
44
Residue number B
112
Peptide name
CD160 antigen

Ligandability

Cysteine 44 of CD160 antigen

Cysteine 112 of CD160 antigen

A redox-regulated disulphide may form within CD160 antigen between cysteines 68 and 113.

Details

Redox score ?
72
PDB code
6ng9
Structure name
crystal structure of human cd160
Structure deposition date
2018-12-21
Thiol separation (Å)
3
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
nan
Peptide accession
O95971
Residue number A
68
Residue number B
113
Peptide name
CD160 antigen

Ligandability

Cysteine 68 of CD160 antigen

Cysteine 113 of CD160 antigen

A redox-regulated disulphide may form within CD160 antigen between cysteines 61 and 113. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
6ng9
Structure name
crystal structure of human cd160
Structure deposition date
2018-12-21
Thiol separation (Å)
5
Half-sphere exposure sum ?
79
Minimum pKa ?
11
% buried
nan
Peptide accession
O95971
Residue number A
61
Residue number B
113
Peptide name
CD160 antigen

Ligandability

Cysteine 61 of CD160 antigen

Cysteine 113 of CD160 antigen

A redox-regulated disulphide may form within CD160 antigen between cysteines 68 and 112. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
6ngg
Structure name
crystal structure of human cd160 v58m mutant
Structure deposition date
2018-12-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95971
Residue number A
68
Residue number B
112
Peptide name
CD160 antigen

Ligandability

Cysteine 68 of CD160 antigen

Cysteine 112 of CD160 antigen

A redox-regulated disulphide may form within CD160 antigen between cysteines 44 and 68. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
6ngg
Structure name
crystal structure of human cd160 v58m mutant
Structure deposition date
2018-12-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95971
Residue number A
44
Residue number B
68
Peptide name
CD160 antigen

Ligandability

Cysteine 44 of CD160 antigen

Cysteine 68 of CD160 antigen

A redox-regulated disulphide may form within CD160 antigen between cysteines 112 and 113. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
6ngg
Structure name
crystal structure of human cd160 v58m mutant
Structure deposition date
2018-12-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
92
Minimum pKa ?
11
% buried
nan
Peptide accession
O95971
Residue number A
112
Residue number B
113
Peptide name
CD160 antigen

Ligandability

Cysteine 112 of CD160 antigen

Cysteine 113 of CD160 antigen

A redox-regulated disulphide may form within CD160 antigen between cysteines 44 and 113. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
6ngg
Structure name
crystal structure of human cd160 v58m mutant
Structure deposition date
2018-12-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
89
Minimum pKa ?
11
% buried
nan
Peptide accession
O95971
Residue number A
44
Residue number B
113
Peptide name
CD160 antigen

Ligandability

Cysteine 44 of CD160 antigen

Cysteine 113 of CD160 antigen

A redox-regulated disulphide may form within CD160 antigen between cysteines 44 and 61. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
6ng9
Structure name
crystal structure of human cd160
Structure deposition date
2018-12-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95971
Residue number A
44
Residue number B
61
Peptide name
CD160 antigen

Ligandability

Cysteine 44 of CD160 antigen

Cysteine 61 of CD160 antigen

A redox-regulated disulphide may form within CD160 antigen between cysteines 61 and 112. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
6ngg
Structure name
crystal structure of human cd160 v58m mutant
Structure deposition date
2018-12-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95971
Residue number A
61
Residue number B
112
Peptide name
CD160 antigen

Ligandability

Cysteine 61 of CD160 antigen

Cysteine 112 of CD160 antigen

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