Beta-defensin 106
Intramolecular
Cysteine 37 and cysteine 54
Cysteine 33 and cysteine 47
Cysteine 26 and cysteine 53
Cysteine 33 and cysteine 53
Cysteine 47 and cysteine 53
Cysteine 26 and cysteine 33
Cysteine 26 and cysteine 47
Cysteine 33 and cysteine 54
Cysteine 47 and cysteine 54
Cysteine 53 and cysteine 54
More...Cysteine 26 and cysteine 54
Cysteine 37 and cysteine 53
2lwl A 17 A 34
A redox-regulated disulphide may form within Beta-defensin 106 between cysteines 37 and 54 (17 and 34 respectively in this structure).
Details
Redox score ?
86
PDB code
2lwl
Structure name
structural basis for the interaction of human β-defensin 6 and its putative chemokine receptor ccr2 and breast cancer microvesicles
Structure deposition date
2012-08-02
Thiol separation (Å)
3
Half-sphere exposure sum ?
50
Minimum pKa ?
9
% buried
0
Peptide accession
Q8N104
Residue number A
37
Residue number B
54
Peptide name
Beta-defensin 106
Ligandability
Cysteine 37 of Beta-defensin 106
Cysteine 54 of Beta-defensin 106
2lwl A 13 A 27
A redox-regulated disulphide may form within Beta-defensin 106 between cysteines 33 and 47 (13 and 27 respectively in this structure).
Details
Redox score ?
85
PDB code
2lwl
Structure name
structural basis for the interaction of human β-defensin 6 and its putative chemokine receptor ccr2 and breast cancer microvesicles
Structure deposition date
2012-08-02
Thiol separation (Å)
3
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
0
Peptide accession
Q8N104
Residue number A
33
Residue number B
47
Peptide name
Beta-defensin 106
Ligandability
Cysteine 33 of Beta-defensin 106
Cysteine 47 of Beta-defensin 106
2lwl A 6 A 33
A redox-regulated disulphide may form within Beta-defensin 106 between cysteines 26 and 53 (6 and 33 respectively in this structure).
Details
Redox score ?
81
PDB code
2lwl
Structure name
structural basis for the interaction of human β-defensin 6 and its putative chemokine receptor ccr2 and breast cancer microvesicles
Structure deposition date
2012-08-02
Thiol separation (Å)
3
Half-sphere exposure sum ?
56
Minimum pKa ?
10
% buried
2
Peptide accession
Q8N104
Residue number A
26
Residue number B
53
Peptide name
Beta-defensin 106
Ligandability
Cysteine 26 of Beta-defensin 106
Cysteine 53 of Beta-defensin 106
2lwl A 13 A 33
A redox-regulated disulphide may form within Beta-defensin 106 between cysteines 33 and 53 (13 and 33 respectively in this structure).
Details
Redox score ?
80
PDB code
2lwl
Structure name
structural basis for the interaction of human β-defensin 6 and its putative chemokine receptor ccr2 and breast cancer microvesicles
Structure deposition date
2012-08-02
Thiol separation (Å)
3
Half-sphere exposure sum ?
64
Minimum pKa ?
9
% buried
2
Peptide accession
Q8N104
Residue number A
33
Residue number B
53
Peptide name
Beta-defensin 106
Ligandability
Cysteine 33 of Beta-defensin 106
Cysteine 53 of Beta-defensin 106
2lwl A 27 A 33
A redox-regulated disulphide may form within Beta-defensin 106 between cysteines 47 and 53 (27 and 33 respectively in this structure).
Details
Redox score ?
73
PDB code
2lwl
Structure name
structural basis for the interaction of human β-defensin 6 and its putative chemokine receptor ccr2 and breast cancer microvesicles
Structure deposition date
2012-08-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
11
% buried
2
Peptide accession
Q8N104
Residue number A
47
Residue number B
53
Peptide name
Beta-defensin 106
Ligandability
Cysteine 47 of Beta-defensin 106
Cysteine 53 of Beta-defensin 106
2lwl A 6 A 13
A redox-regulated disulphide may form within Beta-defensin 106 between cysteines 26 and 33 (6 and 13 respectively in this structure).
Details
Redox score ?
66
PDB code
2lwl
Structure name
structural basis for the interaction of human β-defensin 6 and its putative chemokine receptor ccr2 and breast cancer microvesicles
Structure deposition date
2012-08-02
Thiol separation (Å)
6
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
1
Peptide accession
Q8N104
Residue number A
26
Residue number B
33
Peptide name
Beta-defensin 106
Ligandability
Cysteine 26 of Beta-defensin 106
Cysteine 33 of Beta-defensin 106
2lwl A 6 A 27
A redox-regulated disulphide may form within Beta-defensin 106 between cysteines 26 and 47 (6 and 27 respectively in this structure).
Details
Redox score ?
62
PDB code
2lwl
Structure name
structural basis for the interaction of human β-defensin 6 and its putative chemokine receptor ccr2 and breast cancer microvesicles
Structure deposition date
2012-08-02
Thiol separation (Å)
7
Half-sphere exposure sum ?
46
Minimum pKa ?
10
% buried
1
Peptide accession
Q8N104
Residue number A
26
Residue number B
47
Peptide name
Beta-defensin 106
Ligandability
Cysteine 26 of Beta-defensin 106
Cysteine 47 of Beta-defensin 106
2lwl A 13 A 34
A redox-regulated disulphide may form within Beta-defensin 106 between cysteines 33 and 54 (13 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 ?
55
PDB code
2lwl
Structure name
structural basis for the interaction of human β-defensin 6 and its putative chemokine receptor ccr2 and breast cancer microvesicles
Structure deposition date
2012-08-02
Thiol separation (Å)
8
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
0
Peptide accession
Q8N104
Residue number A
33
Residue number B
54
Peptide name
Beta-defensin 106
Ligandability
Cysteine 33 of Beta-defensin 106
Cysteine 54 of Beta-defensin 106
2lwl A 27 A 34
A redox-regulated disulphide may form within Beta-defensin 106 between cysteines 47 and 54 (27 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 ?
54
PDB code
2lwl
Structure name
structural basis for the interaction of human β-defensin 6 and its putative chemokine receptor ccr2 and breast cancer microvesicles
Structure deposition date
2012-08-02
Thiol separation (Å)
8
Half-sphere exposure sum ?
51
Minimum pKa ?
11
% buried
0
Peptide accession
Q8N104
Residue number A
47
Residue number B
54
Peptide name
Beta-defensin 106
Ligandability
Cysteine 47 of Beta-defensin 106
Cysteine 54 of Beta-defensin 106
2lwl A 33 A 34
A redox-regulated disulphide may form within Beta-defensin 106 between cysteines 53 and 54 (33 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 ?
53
PDB code
2lwl
Structure name
structural basis for the interaction of human β-defensin 6 and its putative chemokine receptor ccr2 and breast cancer microvesicles
Structure deposition date
2012-08-02
Thiol separation (Å)
7
Half-sphere exposure sum ?
61
Minimum pKa ?
11
% buried
2
Peptide accession
Q8N104
Residue number A
53
Residue number B
54
Peptide name
Beta-defensin 106
Ligandability
Cysteine 53 of Beta-defensin 106
Cysteine 54 of Beta-defensin 106
2lwl A 6 A 34
A redox-regulated disulphide may form within Beta-defensin 106 between cysteines 26 and 54 (6 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 ?
52
PDB code
2lwl
Structure name
structural basis for the interaction of human β-defensin 6 and its putative chemokine receptor ccr2 and breast cancer microvesicles
Structure deposition date
2012-08-02
Thiol separation (Å)
8
Half-sphere exposure sum ?
51
Minimum pKa ?
10
% buried
1
Peptide accession
Q8N104
Residue number A
26
Residue number B
54
Peptide name
Beta-defensin 106
Ligandability
Cysteine 26 of Beta-defensin 106
Cysteine 54 of Beta-defensin 106
2lwl A 17 A 33
A redox-regulated disulphide may form within Beta-defensin 106 between cysteines 37 and 53 (17 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 ?
46
PDB code
2lwl
Structure name
structural basis for the interaction of human β-defensin 6 and its putative chemokine receptor ccr2 and breast cancer microvesicles
Structure deposition date
2012-08-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
2
Peptide accession
Q8N104
Residue number A
37
Residue number B
53
Peptide name
Beta-defensin 106
Ligandability
Cysteine 37 of Beta-defensin 106
Cysteine 53 of Beta-defensin 106
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