Amphiregulin
Intramolecular
Cysteine 146 and cysteine 159 L
Cysteine 172 and cysteine 181 L
Cysteine 154 and cysteine 170
Cysteine 154 and cysteine 159 L
Cysteine 159 and cysteine 170 L
Cysteine 146 and cysteine 154 L
Cysteine 170 and cysteine 181
Cysteine 146 and cysteine 170 L
Cysteine 154 and cysteine 181
Cysteine 170 and cysteine 172 L
More...Cysteine 154 and cysteine 172 L
Cysteine 159 and cysteine 181 L
Cysteine 159 and cysteine 172 L
2rnl A 12 A 25
A redox-regulated disulphide may form within Amphiregulin between cysteines 146 and 159 (12 and 25 respectively in this structure).
Details
Redox score ?
88
PDB code
2rnl
Structure name
solution structure of the egf-like domain from human amphiregulin
Structure deposition date
2008-01-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15514
Residue number A
146
Residue number B
159
Peptide name
Amphiregulin
Ligandability
Cysteine 146 of Amphiregulin
Cysteine 159 of Amphiregulin
2rnl A 38 A 47
A redox-regulated disulphide may form within Amphiregulin between cysteines 172 and 181 (38 and 47 respectively in this structure).
Details
Redox score ?
88
PDB code
2rnl
Structure name
solution structure of the egf-like domain from human amphiregulin
Structure deposition date
2008-01-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15514
Residue number A
172
Residue number B
181
Peptide name
Amphiregulin
Ligandability
Cysteine 172 of Amphiregulin
Cysteine 181 of Amphiregulin
2rnl A 20 A 36
A redox-regulated disulphide may form within Amphiregulin between cysteines 154 and 170 (20 and 36 respectively in this structure).
Details
Redox score ?
87
PDB code
2rnl
Structure name
solution structure of the egf-like domain from human amphiregulin
Structure deposition date
2008-01-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15514
Residue number A
154
Residue number B
170
Peptide name
Amphiregulin
Ligandability
Cysteine 154 of Amphiregulin
Cysteine 170 of Amphiregulin
2rnl A 20 A 25
A redox-regulated disulphide may form within Amphiregulin between cysteines 154 and 159 (20 and 25 respectively in this structure).
Details
Redox score ?
83
PDB code
2rnl
Structure name
solution structure of the egf-like domain from human amphiregulin
Structure deposition date
2008-01-11
Thiol separation (Å)
3
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15514
Residue number A
154
Residue number B
159
Peptide name
Amphiregulin
Ligandability
Cysteine 154 of Amphiregulin
Cysteine 159 of Amphiregulin
2rnl A 25 A 36
A redox-regulated disulphide may form within Amphiregulin between cysteines 159 and 170 (25 and 36 respectively in this structure).
Details
Redox score ?
76
PDB code
2rnl
Structure name
solution structure of the egf-like domain from human amphiregulin
Structure deposition date
2008-01-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15514
Residue number A
159
Residue number B
170
Peptide name
Amphiregulin
Ligandability
Cysteine 159 of Amphiregulin
Cysteine 170 of Amphiregulin
2rnl A 12 A 20
A redox-regulated disulphide may form within Amphiregulin between cysteines 146 and 154 (12 and 20 respectively in this structure).
Details
Redox score ?
71
PDB code
2rnl
Structure name
solution structure of the egf-like domain from human amphiregulin
Structure deposition date
2008-01-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15514
Residue number A
146
Residue number B
154
Peptide name
Amphiregulin
Ligandability
Cysteine 146 of Amphiregulin
Cysteine 154 of Amphiregulin
2rnl A 36 A 47
A redox-regulated disulphide may form within Amphiregulin between cysteines 170 and 181 (36 and 47 respectively in this structure).
Details
Redox score ?
66
PDB code
2rnl
Structure name
solution structure of the egf-like domain from human amphiregulin
Structure deposition date
2008-01-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15514
Residue number A
170
Residue number B
181
Peptide name
Amphiregulin
Ligandability
Cysteine 170 of Amphiregulin
Cysteine 181 of Amphiregulin
2rnl A 12 A 36
A redox-regulated disulphide may form within Amphiregulin between cysteines 146 and 170 (12 and 36 respectively in this structure).
Details
Redox score ?
65
PDB code
2rnl
Structure name
solution structure of the egf-like domain from human amphiregulin
Structure deposition date
2008-01-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15514
Residue number A
146
Residue number B
170
Peptide name
Amphiregulin
Ligandability
Cysteine 146 of Amphiregulin
Cysteine 170 of Amphiregulin
2rnl A 20 A 47
A redox-regulated disulphide may form within Amphiregulin between cysteines 154 and 181 (20 and 47 respectively in this structure).
Details
Redox score ?
61
PDB code
2rnl
Structure name
solution structure of the egf-like domain from human amphiregulin
Structure deposition date
2008-01-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15514
Residue number A
154
Residue number B
181
Peptide name
Amphiregulin
Ligandability
Cysteine 154 of Amphiregulin
Cysteine 181 of Amphiregulin
2rnl A 36 A 38
A redox-regulated disulphide may form within Amphiregulin between cysteines 170 and 172 (36 and 38 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
2rnl
Structure name
solution structure of the egf-like domain from human amphiregulin
Structure deposition date
2008-01-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15514
Residue number A
170
Residue number B
172
Peptide name
Amphiregulin
Ligandability
Cysteine 170 of Amphiregulin
Cysteine 172 of Amphiregulin
2rnl A 20 A 38
A redox-regulated disulphide may form within Amphiregulin between cysteines 154 and 172 (20 and 38 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
2rnl
Structure name
solution structure of the egf-like domain from human amphiregulin
Structure deposition date
2008-01-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15514
Residue number A
154
Residue number B
172
Peptide name
Amphiregulin
Ligandability
Cysteine 154 of Amphiregulin
Cysteine 172 of Amphiregulin
2rnl A 25 A 47
A redox-regulated disulphide may form within Amphiregulin between cysteines 159 and 181 (25 and 47 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
2rnl
Structure name
solution structure of the egf-like domain from human amphiregulin
Structure deposition date
2008-01-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15514
Residue number A
159
Residue number B
181
Peptide name
Amphiregulin
Ligandability
Cysteine 159 of Amphiregulin
Cysteine 181 of Amphiregulin
2rnl A 25 A 38
A redox-regulated disulphide may form within Amphiregulin between cysteines 159 and 172 (25 and 38 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
2rnl
Structure name
solution structure of the egf-like domain from human amphiregulin
Structure deposition date
2008-01-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15514
Residue number A
159
Residue number B
172
Peptide name
Amphiregulin
Ligandability
Cysteine 159 of Amphiregulin
Cysteine 172 of Amphiregulin
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