ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Beta-defensin 103

Intramolecular
Cysteine 45 and cysteine 63
Cysteine 33 and cysteine 62
Cysteine 40 and cysteine 55
Cysteine 33 and cysteine 55
Cysteine 55 and cysteine 62
Cysteine 33 and cysteine 40
Cysteine 40 and cysteine 62
Cysteine 62 and cysteine 63
Cysteine 45 and cysteine 62
Cysteine 55 and cysteine 63
More...
Cysteine 45 and cysteine 55
Cysteine 40 and cysteine 63
Cysteine 33 and cysteine 63
Cysteine 33 and cysteine 45
Cysteine 40 and cysteine 45
A redox-regulated disulphide may form within Beta-defensin 103 between cysteines 45 and 63 (23 and 41 respectively in this structure).

Details

Redox score ?
87
PDB code
1kj6
Structure name
solution structure of human beta-defensin 3
Structure deposition date
2001-12-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81534
Residue number A
45
Residue number B
63
Peptide name
Beta-defensin 103

Ligandability

Cysteine 45 of Beta-defensin 103

Cysteine 63 of Beta-defensin 103

A redox-regulated disulphide may form within Beta-defensin 103 between cysteines 33 and 62 (11 and 40 respectively in this structure).

Details

Redox score ?
85
PDB code
1kj6
Structure name
solution structure of human beta-defensin 3
Structure deposition date
2001-12-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81534
Residue number A
33
Residue number B
62
Peptide name
Beta-defensin 103

Ligandability

Cysteine 33 of Beta-defensin 103

Cysteine 62 of Beta-defensin 103

A redox-regulated disulphide may form within Beta-defensin 103 between cysteines 40 and 55 (18 and 33 respectively in this structure).

Details

Redox score ?
85
PDB code
1kj6
Structure name
solution structure of human beta-defensin 3
Structure deposition date
2001-12-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81534
Residue number A
40
Residue number B
55
Peptide name
Beta-defensin 103

Ligandability

Cysteine 40 of Beta-defensin 103

Cysteine 55 of Beta-defensin 103

A redox-regulated disulphide may form within Beta-defensin 103 between cysteines 33 and 55 (11 and 33 respectively in this structure).

Details

Redox score ?
79
PDB code
1kj6
Structure name
solution structure of human beta-defensin 3
Structure deposition date
2001-12-04
Thiol separation (Å)
3
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81534
Residue number A
33
Residue number B
55
Peptide name
Beta-defensin 103

Ligandability

Cysteine 33 of Beta-defensin 103

Cysteine 55 of Beta-defensin 103

A redox-regulated disulphide may form within Beta-defensin 103 between cysteines 55 and 62 (33 and 40 respectively in this structure).

Details

Redox score ?
74
PDB code
1kj6
Structure name
solution structure of human beta-defensin 3
Structure deposition date
2001-12-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81534
Residue number A
55
Residue number B
62
Peptide name
Beta-defensin 103

Ligandability

Cysteine 55 of Beta-defensin 103

Cysteine 62 of Beta-defensin 103

A redox-regulated disulphide may form within Beta-defensin 103 between cysteines 33 and 40 (11 and 18 respectively in this structure).

Details

Redox score ?
71
PDB code
1kj6
Structure name
solution structure of human beta-defensin 3
Structure deposition date
2001-12-04
Thiol separation (Å)
5
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81534
Residue number A
33
Residue number B
40
Peptide name
Beta-defensin 103

Ligandability

Cysteine 33 of Beta-defensin 103

Cysteine 40 of Beta-defensin 103

A redox-regulated disulphide may form within Beta-defensin 103 between cysteines 40 and 62 (18 and 40 respectively in this structure).

Details

Redox score ?
66
PDB code
1kj6
Structure name
solution structure of human beta-defensin 3
Structure deposition date
2001-12-04
Thiol separation (Å)
5
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81534
Residue number A
40
Residue number B
62
Peptide name
Beta-defensin 103

Ligandability

Cysteine 40 of Beta-defensin 103

Cysteine 62 of Beta-defensin 103

A redox-regulated disulphide may form within Beta-defensin 103 between cysteines 62 and 63 (40 and 41 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
1kj6
Structure name
solution structure of human beta-defensin 3
Structure deposition date
2001-12-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81534
Residue number A
62
Residue number B
63
Peptide name
Beta-defensin 103

Ligandability

Cysteine 62 of Beta-defensin 103

Cysteine 63 of Beta-defensin 103

A redox-regulated disulphide may form within Beta-defensin 103 between cysteines 45 and 62 (23 and 40 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
1kj6
Structure name
solution structure of human beta-defensin 3
Structure deposition date
2001-12-04
Thiol separation (Å)
7
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81534
Residue number A
45
Residue number B
62
Peptide name
Beta-defensin 103

Ligandability

Cysteine 45 of Beta-defensin 103

Cysteine 62 of Beta-defensin 103

A redox-regulated disulphide may form within Beta-defensin 103 between cysteines 55 and 63 (33 and 41 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
1kj6
Structure name
solution structure of human beta-defensin 3
Structure deposition date
2001-12-04
Thiol separation (Å)
7
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81534
Residue number A
55
Residue number B
63
Peptide name
Beta-defensin 103

Ligandability

Cysteine 55 of Beta-defensin 103

Cysteine 63 of Beta-defensin 103

A redox-regulated disulphide may form within Beta-defensin 103 between cysteines 45 and 55 (23 and 33 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
1kj6
Structure name
solution structure of human beta-defensin 3
Structure deposition date
2001-12-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81534
Residue number A
45
Residue number B
55
Peptide name
Beta-defensin 103

Ligandability

Cysteine 45 of Beta-defensin 103

Cysteine 55 of Beta-defensin 103

A redox-regulated disulphide may form within Beta-defensin 103 between cysteines 40 and 63 (18 and 41 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
1kj6
Structure name
solution structure of human beta-defensin 3
Structure deposition date
2001-12-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81534
Residue number A
40
Residue number B
63
Peptide name
Beta-defensin 103

Ligandability

Cysteine 40 of Beta-defensin 103

Cysteine 63 of Beta-defensin 103

A redox-regulated disulphide may form within Beta-defensin 103 between cysteines 33 and 63 (11 and 41 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
1kj6
Structure name
solution structure of human beta-defensin 3
Structure deposition date
2001-12-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81534
Residue number A
33
Residue number B
63
Peptide name
Beta-defensin 103

Ligandability

Cysteine 33 of Beta-defensin 103

Cysteine 63 of Beta-defensin 103

A redox-regulated disulphide may form within Beta-defensin 103 between cysteines 33 and 45 (11 and 23 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
1kj6
Structure name
solution structure of human beta-defensin 3
Structure deposition date
2001-12-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81534
Residue number A
33
Residue number B
45
Peptide name
Beta-defensin 103

Ligandability

Cysteine 33 of Beta-defensin 103

Cysteine 45 of Beta-defensin 103

A redox-regulated disulphide may form within Beta-defensin 103 between cysteines 40 and 45 (18 and 23 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
1kj6
Structure name
solution structure of human beta-defensin 3
Structure deposition date
2001-12-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81534
Residue number A
40
Residue number B
45
Peptide name
Beta-defensin 103

Ligandability

Cysteine 40 of Beta-defensin 103

Cysteine 45 of Beta-defensin 103

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