ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Myelin-associated glycoprotein

Intramolecular
Cysteine 347 and cysteine 392
Cysteine 42 and cysteine 100
Cysteine 421 and cysteine 430
Cysteine 261 and cysteine 305
Cysteine 432 and cysteine 488
Cysteine 159 and cysteine 217
Cysteine 37 and cysteine 165
Cysteine 421 and cysteine 488
Cysteine 421 and cysteine 432
Cysteine 430 and cysteine 432
Cysteine 430 and cysteine 488
A redox-regulated disulphide may form within Myelin-associated glycoprotein between cysteines 347 and 392.

Details

Redox score ?
84
PDB code
5lf5
Structure name
myelin-associated glycoprotein (mag) deglycosylated full extracellular domain with co-purified ligand
Structure deposition date
2016-06-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20917
Residue number A
347
Residue number B
392
Peptide name
Myelin-associated glycoprotein

Ligandability

Cysteine 347 of Myelin-associated glycoprotein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 392 of Myelin-associated glycoprotein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Myelin-associated glycoprotein between cysteines 42 and 100.

Details

Redox score ?
83
PDB code
5lfv
Structure name
crystal structure of glycosylated myelin-associated glycoprotein (mag) ig1-3 with soaked trisaccharide ligand
Structure deposition date
2016-07-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20917
Residue number A
42
Residue number B
100
Peptide name
Myelin-associated glycoprotein

Ligandability

Cysteine 42 of Myelin-associated glycoprotein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 100 of Myelin-associated glycoprotein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Myelin-associated glycoprotein between cysteines 421 and 430.

Details

Redox score ?
82
PDB code
5lf5
Structure name
myelin-associated glycoprotein (mag) deglycosylated full extracellular domain with co-purified ligand
Structure deposition date
2016-06-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20917
Residue number A
421
Residue number B
430
Peptide name
Myelin-associated glycoprotein

Ligandability

Cysteine 421 of Myelin-associated glycoprotein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 430 of Myelin-associated glycoprotein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Myelin-associated glycoprotein between cysteines 261 and 305.

Details

Redox score ?
82
PDB code
5lfv
Structure name
crystal structure of glycosylated myelin-associated glycoprotein (mag) ig1-3 with soaked trisaccharide ligand
Structure deposition date
2016-07-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20917
Residue number A
261
Residue number B
305
Peptide name
Myelin-associated glycoprotein

Ligandability

Cysteine 261 of Myelin-associated glycoprotein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 305 of Myelin-associated glycoprotein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Myelin-associated glycoprotein between cysteines 432 and 488.

Details

Redox score ?
82
PDB code
5lfu
Structure name
myelin-associated glycoprotein (mag) glycosylated and lysine- methylated full extracellular domain
Structure deposition date
2016-07-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20917
Residue number A
432
Residue number B
488
Peptide name
Myelin-associated glycoprotein

Ligandability

Cysteine 432 of Myelin-associated glycoprotein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 488 of Myelin-associated glycoprotein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Myelin-associated glycoprotein between cysteines 159 and 217.

Details

Redox score ?
82
PDB code
5lfu
Structure name
myelin-associated glycoprotein (mag) glycosylated and lysine- methylated full extracellular domain
Structure deposition date
2016-07-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20917
Residue number A
159
Residue number B
217
Peptide name
Myelin-associated glycoprotein

Ligandability

Cysteine 159 of Myelin-associated glycoprotein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 217 of Myelin-associated glycoprotein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Myelin-associated glycoprotein between cysteines 37 and 165.

Details

Redox score ?
81
PDB code
5lfu
Structure name
myelin-associated glycoprotein (mag) glycosylated and lysine- methylated full extracellular domain
Structure deposition date
2016-07-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20917
Residue number A
37
Residue number B
165
Peptide name
Myelin-associated glycoprotein

Ligandability

Cysteine 37 of Myelin-associated glycoprotein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 165 of Myelin-associated glycoprotein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Myelin-associated glycoprotein between cysteines 421 and 488. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
5lf5
Structure name
myelin-associated glycoprotein (mag) deglycosylated full extracellular domain with co-purified ligand
Structure deposition date
2016-06-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20917
Residue number A
421
Residue number B
488
Peptide name
Myelin-associated glycoprotein

Ligandability

Cysteine 421 of Myelin-associated glycoprotein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 488 of Myelin-associated glycoprotein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Myelin-associated glycoprotein between cysteines 421 and 432. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
5lfu
Structure name
myelin-associated glycoprotein (mag) glycosylated and lysine- methylated full extracellular domain
Structure deposition date
2016-07-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20917
Residue number A
421
Residue number B
432
Peptide name
Myelin-associated glycoprotein

Ligandability

Cysteine 421 of Myelin-associated glycoprotein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 432 of Myelin-associated glycoprotein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Myelin-associated glycoprotein between cysteines 430 and 432. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
5lfu
Structure name
myelin-associated glycoprotein (mag) glycosylated and lysine- methylated full extracellular domain
Structure deposition date
2016-07-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20917
Residue number A
430
Residue number B
432
Peptide name
Myelin-associated glycoprotein

Ligandability

Cysteine 430 of Myelin-associated glycoprotein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 432 of Myelin-associated glycoprotein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Myelin-associated glycoprotein between cysteines 430 and 488. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
5lfu
Structure name
myelin-associated glycoprotein (mag) glycosylated and lysine- methylated full extracellular domain
Structure deposition date
2016-07-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20917
Residue number A
430
Residue number B
488
Peptide name
Myelin-associated glycoprotein

Ligandability

Cysteine 430 of Myelin-associated glycoprotein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 488 of Myelin-associated glycoprotein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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