ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Protein amnionless

Intramolecular
Cysteine 205 and cysteine 211
Cysteine 234 and cysteine 250
Cysteine 43 and cysteine 96
Cysteine 239 and cysteine 253
Cysteine 223 and cysteine 249
Cysteine 137 and cysteine 213
Cysteine 234 and cysteine 249
Cysteine 249 and cysteine 250
Cysteine 223 and cysteine 234
Cysteine 223 and cysteine 250
A redox-regulated disulphide may form within Protein amnionless between cysteines 205 and 211.

Details

Redox score ?
86
PDB code
6gje
Structure name
structure of the amnionless(20-357)-cubilin(36-135) complex
Structure deposition date
2018-05-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BXJ7
Residue number A
205
Residue number B
211
Peptide name
Protein amnionless

Ligandability

Cysteine 205 of Protein amnionless

Cysteine 211 of Protein amnionless

A redox-regulated disulphide may form within Protein amnionless between cysteines 234 and 250.

Details

Redox score ?
85
PDB code
6gje
Structure name
structure of the amnionless(20-357)-cubilin(36-135) complex
Structure deposition date
2018-05-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BXJ7
Residue number A
234
Residue number B
250
Peptide name
Protein amnionless

Ligandability

Cysteine 234 of Protein amnionless

Cysteine 250 of Protein amnionless

A redox-regulated disulphide may form within Protein amnionless between cysteines 43 and 96.

Details

Redox score ?
85
PDB code
6gje
Structure name
structure of the amnionless(20-357)-cubilin(36-135) complex
Structure deposition date
2018-05-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BXJ7
Residue number A
43
Residue number B
96
Peptide name
Protein amnionless

Ligandability

Cysteine 43 of Protein amnionless

Cysteine 96 of Protein amnionless

A redox-regulated disulphide may form within Protein amnionless between cysteines 239 and 253.

Details

Redox score ?
82
PDB code
6gje
Structure name
structure of the amnionless(20-357)-cubilin(36-135) complex
Structure deposition date
2018-05-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BXJ7
Residue number A
239
Residue number B
253
Peptide name
Protein amnionless

Ligandability

Cysteine 239 of Protein amnionless

Cysteine 253 of Protein amnionless

A redox-regulated disulphide may form within Protein amnionless between cysteines 223 and 249.

Details

Redox score ?
81
PDB code
6gje
Structure name
structure of the amnionless(20-357)-cubilin(36-135) complex
Structure deposition date
2018-05-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BXJ7
Residue number A
223
Residue number B
249
Peptide name
Protein amnionless

Ligandability

Cysteine 223 of Protein amnionless

Cysteine 249 of Protein amnionless

A redox-regulated disulphide may form within Protein amnionless between cysteines 137 and 213.

Details

Redox score ?
81
PDB code
6gje
Structure name
structure of the amnionless(20-357)-cubilin(36-135) complex
Structure deposition date
2018-05-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BXJ7
Residue number A
137
Residue number B
213
Peptide name
Protein amnionless

Ligandability

Cysteine 137 of Protein amnionless

Cysteine 213 of Protein amnionless

A redox-regulated disulphide may form within Protein amnionless between cysteines 234 and 249.

Details

Redox score ?
61
PDB code
6gje
Structure name
structure of the amnionless(20-357)-cubilin(36-135) complex
Structure deposition date
2018-05-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BXJ7
Residue number A
234
Residue number B
249
Peptide name
Protein amnionless

Ligandability

Cysteine 234 of Protein amnionless

Cysteine 249 of Protein amnionless

A redox-regulated disulphide may form within Protein amnionless between cysteines 249 and 250.

Details

Redox score ?
60
PDB code
6gje
Structure name
structure of the amnionless(20-357)-cubilin(36-135) complex
Structure deposition date
2018-05-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BXJ7
Residue number A
249
Residue number B
250
Peptide name
Protein amnionless

Ligandability

Cysteine 249 of Protein amnionless

Cysteine 250 of Protein amnionless

A redox-regulated disulphide may form within Protein amnionless between cysteines 223 and 234. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
6gje
Structure name
structure of the amnionless(20-357)-cubilin(36-135) complex
Structure deposition date
2018-05-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BXJ7
Residue number A
223
Residue number B
234
Peptide name
Protein amnionless

Ligandability

Cysteine 223 of Protein amnionless

Cysteine 234 of Protein amnionless

A redox-regulated disulphide may form within Protein amnionless between cysteines 223 and 250. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
6gje
Structure name
structure of the amnionless(20-357)-cubilin(36-135) complex
Structure deposition date
2018-05-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BXJ7
Residue number A
223
Residue number B
250
Peptide name
Protein amnionless

Ligandability

Cysteine 223 of Protein amnionless

Cysteine 250 of Protein amnionless

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