ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Pro-neuregulin-1, membrane-bound isoform

Intramolecular
Cysteine 182 and cysteine 196
Cysteine 190 and cysteine 210
Cysteine 212 and cysteine 221
Cysteine 57 and cysteine 112
Cysteine 196 and cysteine 210
Cysteine 190 and cysteine 212
Cysteine 210 and cysteine 212
Cysteine 190 and cysteine 196
Cysteine 190 and cysteine 221
Cysteine 182 and cysteine 210
More...
Cysteine 210 and cysteine 221
Cysteine 182 and cysteine 190
Cysteine 196 and cysteine 212
Cysteine 182 and cysteine 212
Cysteine 196 and cysteine 221
A redox-regulated disulphide may form within Pro-neuregulin-1, membrane-bound isoform between cysteines 182 and 196 (6 and 20 respectively in this structure).

Details

Redox score ?
88
PDB code
1hae
Structure name
heregulin-alpha epidermal growth factor-like domain, nmr, 20 structures
Structure deposition date
1995-11-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q02297
Residue number A
182
Residue number B
196
Peptide name
Pro-neuregulin-1, membrane-bound isoform

Ligandability

Cysteine 182 of Pro-neuregulin-1, membrane-bound isoform

Cysteine 196 of Pro-neuregulin-1, membrane-bound isoform

A redox-regulated disulphide may form within Pro-neuregulin-1, membrane-bound isoform between cysteines 190 and 210 (14 and 34 respectively in this structure).

Details

Redox score ?
87
PDB code
1hae
Structure name
heregulin-alpha epidermal growth factor-like domain, nmr, 20 structures
Structure deposition date
1995-11-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q02297
Residue number A
190
Residue number B
210
Peptide name
Pro-neuregulin-1, membrane-bound isoform

Ligandability

Cysteine 190 of Pro-neuregulin-1, membrane-bound isoform

Cysteine 210 of Pro-neuregulin-1, membrane-bound isoform

A redox-regulated disulphide may form within Pro-neuregulin-1, membrane-bound isoform between cysteines 212 and 221.

Details

Redox score ?
87
PDB code
1hrf
Structure name
solution structure of the epidermal growth factor-like domain of heregulin-alpha, a ligand for p180erb4
Structure deposition date
1994-07-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q02297
Residue number A
212
Residue number B
221
Peptide name
Pro-neuregulin-1, membrane-bound isoform

Ligandability

Cysteine 212 of Pro-neuregulin-1, membrane-bound isoform

Cysteine 221 of Pro-neuregulin-1, membrane-bound isoform

A redox-regulated disulphide may form within Pro-neuregulin-1, membrane-bound isoform between cysteines 57 and 112 (42 and 97 respectively in this structure).

Details

Redox score ?
81
PDB code
7sjl
Structure name
solution nmr structure of immunoglobulin-like domain of human neuregulin-1
Structure deposition date
2021-10-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q02297
Residue number A
57
Residue number B
112
Peptide name
Pro-neuregulin-1, membrane-bound isoform

Ligandability

Cysteine 57 of Pro-neuregulin-1, membrane-bound isoform

Cysteine 112 of Pro-neuregulin-1, membrane-bound isoform

A redox-regulated disulphide may form within Pro-neuregulin-1, membrane-bound isoform between cysteines 196 and 210 (20 and 34 respectively in this structure).

Details

Redox score ?
74
PDB code
1haf
Structure name
heregulin-alpha epidermal growth factor-like domain, nmr, minimized average structure
Structure deposition date
1995-11-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q02297
Residue number A
196
Residue number B
210
Peptide name
Pro-neuregulin-1, membrane-bound isoform

Ligandability

Cysteine 196 of Pro-neuregulin-1, membrane-bound isoform

Cysteine 210 of Pro-neuregulin-1, membrane-bound isoform

A redox-regulated disulphide may form within Pro-neuregulin-1, membrane-bound isoform between cysteines 190 and 212 (14 and 36 respectively in this structure).

Details

Redox score ?
74
PDB code
1haf
Structure name
heregulin-alpha epidermal growth factor-like domain, nmr, minimized average structure
Structure deposition date
1995-11-30
Thiol separation (Å)
5
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q02297
Residue number A
190
Residue number B
212
Peptide name
Pro-neuregulin-1, membrane-bound isoform

Ligandability

Cysteine 190 of Pro-neuregulin-1, membrane-bound isoform

Cysteine 212 of Pro-neuregulin-1, membrane-bound isoform

A redox-regulated disulphide may form within Pro-neuregulin-1, membrane-bound isoform between cysteines 210 and 212 (34 and 36 respectively in this structure).

Details

Redox score ?
73
PDB code
1haf
Structure name
heregulin-alpha epidermal growth factor-like domain, nmr, minimized average structure
Structure deposition date
1995-11-30
Thiol separation (Å)
5
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q02297
Residue number A
210
Residue number B
212
Peptide name
Pro-neuregulin-1, membrane-bound isoform

Ligandability

Cysteine 210 of Pro-neuregulin-1, membrane-bound isoform

Cysteine 212 of Pro-neuregulin-1, membrane-bound isoform

A redox-regulated disulphide may form within Pro-neuregulin-1, membrane-bound isoform between cysteines 190 and 196.

Details

Redox score ?
71
PDB code
1hre
Structure name
solution structure of the epidermal growth factor-like domain of heregulin-alpha, a ligand for p180erb4
Structure deposition date
1994-07-21
Thiol separation (Å)
5
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q02297
Residue number A
190
Residue number B
196
Peptide name
Pro-neuregulin-1, membrane-bound isoform

Ligandability

Cysteine 190 of Pro-neuregulin-1, membrane-bound isoform

Cysteine 196 of Pro-neuregulin-1, membrane-bound isoform

A redox-regulated disulphide may form within Pro-neuregulin-1, membrane-bound isoform between cysteines 190 and 221 (14 and 45 respectively in this structure).

Details

Redox score ?
71
PDB code
1hae
Structure name
heregulin-alpha epidermal growth factor-like domain, nmr, 20 structures
Structure deposition date
1995-11-30
Thiol separation (Å)
5
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q02297
Residue number A
190
Residue number B
221
Peptide name
Pro-neuregulin-1, membrane-bound isoform

Ligandability

Cysteine 190 of Pro-neuregulin-1, membrane-bound isoform

Cysteine 221 of Pro-neuregulin-1, membrane-bound isoform

A redox-regulated disulphide may form within Pro-neuregulin-1, membrane-bound isoform between cysteines 182 and 210 (6 and 34 respectively in this structure).

Details

Redox score ?
68
PDB code
1haf
Structure name
heregulin-alpha epidermal growth factor-like domain, nmr, minimized average structure
Structure deposition date
1995-11-30
Thiol separation (Å)
6
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q02297
Residue number A
182
Residue number B
210
Peptide name
Pro-neuregulin-1, membrane-bound isoform

Ligandability

Cysteine 182 of Pro-neuregulin-1, membrane-bound isoform

Cysteine 210 of Pro-neuregulin-1, membrane-bound isoform

A redox-regulated disulphide may form within Pro-neuregulin-1, membrane-bound isoform between cysteines 210 and 221.

Details

Redox score ?
64
PDB code
1hre
Structure name
solution structure of the epidermal growth factor-like domain of heregulin-alpha, a ligand for p180erb4
Structure deposition date
1994-07-21
Thiol separation (Å)
6
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q02297
Residue number A
210
Residue number B
221
Peptide name
Pro-neuregulin-1, membrane-bound isoform

Ligandability

Cysteine 210 of Pro-neuregulin-1, membrane-bound isoform

Cysteine 221 of Pro-neuregulin-1, membrane-bound isoform

A redox-regulated disulphide may form within Pro-neuregulin-1, membrane-bound isoform between cysteines 182 and 190. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
1hrf
Structure name
solution structure of the epidermal growth factor-like domain of heregulin-alpha, a ligand for p180erb4
Structure deposition date
1994-07-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q02297
Residue number A
182
Residue number B
190
Peptide name
Pro-neuregulin-1, membrane-bound isoform

Ligandability

Cysteine 182 of Pro-neuregulin-1, membrane-bound isoform

Cysteine 190 of Pro-neuregulin-1, membrane-bound isoform

A redox-regulated disulphide may form within Pro-neuregulin-1, membrane-bound isoform between cysteines 196 and 212 (20 and 36 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
1hae
Structure name
heregulin-alpha epidermal growth factor-like domain, nmr, 20 structures
Structure deposition date
1995-11-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q02297
Residue number A
196
Residue number B
212
Peptide name
Pro-neuregulin-1, membrane-bound isoform

Ligandability

Cysteine 196 of Pro-neuregulin-1, membrane-bound isoform

Cysteine 212 of Pro-neuregulin-1, membrane-bound isoform

A redox-regulated disulphide may form within Pro-neuregulin-1, membrane-bound isoform between cysteines 182 and 212 (6 and 36 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
1hae
Structure name
heregulin-alpha epidermal growth factor-like domain, nmr, 20 structures
Structure deposition date
1995-11-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q02297
Residue number A
182
Residue number B
212
Peptide name
Pro-neuregulin-1, membrane-bound isoform

Ligandability

Cysteine 182 of Pro-neuregulin-1, membrane-bound isoform

Cysteine 212 of Pro-neuregulin-1, membrane-bound isoform

A redox-regulated disulphide may form within Pro-neuregulin-1, membrane-bound isoform between cysteines 196 and 221 (20 and 45 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
1hae
Structure name
heregulin-alpha epidermal growth factor-like domain, nmr, 20 structures
Structure deposition date
1995-11-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q02297
Residue number A
196
Residue number B
221
Peptide name
Pro-neuregulin-1, membrane-bound isoform

Ligandability

Cysteine 196 of Pro-neuregulin-1, membrane-bound isoform

Cysteine 221 of Pro-neuregulin-1, membrane-bound isoform

If this tool was useful for finding a disulphide, please cite: