ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Amphoterin-induced protein 1

Intramolecular
Cysteine 227 and cysteine 270
Cysteine 38 and cysteine 47
Cysteine 290 and cysteine 340
Cysteine 34 and cysteine 40
Cysteine 225 and cysteine 253
Cysteine 34 and cysteine 38
Cysteine 38 and cysteine 40
Cysteine 40 and cysteine 47
Cysteine 34 and cysteine 47
Cysteine 225 and cysteine 270
More...
Cysteine 253 and cysteine 270
Cysteine 225 and cysteine 227
Cysteine 227 and cysteine 253
A redox-regulated disulphide may form within Amphoterin-induced protein 1 between cysteines 227 and 270.

Details

Redox score ?
87
PDB code
2xot
Structure name
crystal structure of neuronal leucine rich repeat protein amigo-1
Structure deposition date
2010-08-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q80ZD8
Residue number A
227
Residue number B
270
Peptide name
Amphoterin-induced protein 1

Ligandability

Cysteine 227 of Amphoterin-induced protein 1

Cysteine 270 of Amphoterin-induced protein 1

A redox-regulated disulphide may form within Amphoterin-induced protein 1 between cysteines 38 and 47.

Details

Redox score ?
85
PDB code
2xot
Structure name
crystal structure of neuronal leucine rich repeat protein amigo-1
Structure deposition date
2010-08-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q80ZD8
Residue number A
38
Residue number B
47
Peptide name
Amphoterin-induced protein 1

Ligandability

Cysteine 38 of Amphoterin-induced protein 1

Cysteine 47 of Amphoterin-induced protein 1

A redox-regulated disulphide may form within Amphoterin-induced protein 1 between cysteines 290 and 340.

Details

Redox score ?
84
PDB code
2xot
Structure name
crystal structure of neuronal leucine rich repeat protein amigo-1
Structure deposition date
2010-08-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q80ZD8
Residue number A
290
Residue number B
340
Peptide name
Amphoterin-induced protein 1

Ligandability

Cysteine 290 of Amphoterin-induced protein 1

Cysteine 340 of Amphoterin-induced protein 1

A redox-regulated disulphide may form within Amphoterin-induced protein 1 between cysteines 34 and 40.

Details

Redox score ?
83
PDB code
2xot
Structure name
crystal structure of neuronal leucine rich repeat protein amigo-1
Structure deposition date
2010-08-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q80ZD8
Residue number A
34
Residue number B
40
Peptide name
Amphoterin-induced protein 1

Ligandability

Cysteine 34 of Amphoterin-induced protein 1

Cysteine 40 of Amphoterin-induced protein 1

A redox-regulated disulphide may form within Amphoterin-induced protein 1 between cysteines 225 and 253.

Details

Redox score ?
83
PDB code
2xot
Structure name
crystal structure of neuronal leucine rich repeat protein amigo-1
Structure deposition date
2010-08-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q80ZD8
Residue number A
225
Residue number B
253
Peptide name
Amphoterin-induced protein 1

Ligandability

Cysteine 225 of Amphoterin-induced protein 1

Cysteine 253 of Amphoterin-induced protein 1

A redox-regulated disulphide may form within Amphoterin-induced protein 1 between cysteines 34 and 38.

Details

Redox score ?
67
PDB code
2xot
Structure name
crystal structure of neuronal leucine rich repeat protein amigo-1
Structure deposition date
2010-08-23
Thiol separation (Å)
6
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q80ZD8
Residue number A
34
Residue number B
38
Peptide name
Amphoterin-induced protein 1

Ligandability

Cysteine 34 of Amphoterin-induced protein 1

Cysteine 38 of Amphoterin-induced protein 1

A redox-regulated disulphide may form within Amphoterin-induced protein 1 between cysteines 38 and 40.

Details

Redox score ?
65
PDB code
2xot
Structure name
crystal structure of neuronal leucine rich repeat protein amigo-1
Structure deposition date
2010-08-23
Thiol separation (Å)
5
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q80ZD8
Residue number A
38
Residue number B
40
Peptide name
Amphoterin-induced protein 1

Ligandability

Cysteine 38 of Amphoterin-induced protein 1

Cysteine 40 of Amphoterin-induced protein 1

A redox-regulated disulphide may form within Amphoterin-induced protein 1 between cysteines 40 and 47. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
2xot
Structure name
crystal structure of neuronal leucine rich repeat protein amigo-1
Structure deposition date
2010-08-23
Thiol separation (Å)
6
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q80ZD8
Residue number A
40
Residue number B
47
Peptide name
Amphoterin-induced protein 1

Ligandability

Cysteine 40 of Amphoterin-induced protein 1

Cysteine 47 of Amphoterin-induced protein 1

A redox-regulated disulphide may form within Amphoterin-induced protein 1 between cysteines 34 and 47. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
2xot
Structure name
crystal structure of neuronal leucine rich repeat protein amigo-1
Structure deposition date
2010-08-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q80ZD8
Residue number A
34
Residue number B
47
Peptide name
Amphoterin-induced protein 1

Ligandability

Cysteine 34 of Amphoterin-induced protein 1

Cysteine 47 of Amphoterin-induced protein 1

A redox-regulated disulphide may form within Amphoterin-induced protein 1 between cysteines 225 and 270. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
2xot
Structure name
crystal structure of neuronal leucine rich repeat protein amigo-1
Structure deposition date
2010-08-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q80ZD8
Residue number A
225
Residue number B
270
Peptide name
Amphoterin-induced protein 1

Ligandability

Cysteine 225 of Amphoterin-induced protein 1

Cysteine 270 of Amphoterin-induced protein 1

A redox-regulated disulphide may form within Amphoterin-induced protein 1 between cysteines 253 and 270. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
2xot
Structure name
crystal structure of neuronal leucine rich repeat protein amigo-1
Structure deposition date
2010-08-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q80ZD8
Residue number A
253
Residue number B
270
Peptide name
Amphoterin-induced protein 1

Ligandability

Cysteine 253 of Amphoterin-induced protein 1

Cysteine 270 of Amphoterin-induced protein 1

A redox-regulated disulphide may form within Amphoterin-induced protein 1 between cysteines 225 and 227. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
2xot
Structure name
crystal structure of neuronal leucine rich repeat protein amigo-1
Structure deposition date
2010-08-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q80ZD8
Residue number A
225
Residue number B
227
Peptide name
Amphoterin-induced protein 1

Ligandability

Cysteine 225 of Amphoterin-induced protein 1

Cysteine 227 of Amphoterin-induced protein 1

A redox-regulated disulphide may form within Amphoterin-induced protein 1 between cysteines 227 and 253. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
2xot
Structure name
crystal structure of neuronal leucine rich repeat protein amigo-1
Structure deposition date
2010-08-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q80ZD8
Residue number A
227
Residue number B
253
Peptide name
Amphoterin-induced protein 1

Ligandability

Cysteine 227 of Amphoterin-induced protein 1

Cysteine 253 of Amphoterin-induced protein 1

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