ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Ephrin-A5

Intramolecular
Cysteine 62 and cysteine 102
Cysteine 53 and cysteine 164
Cysteine 90 and cysteine 151
A redox-regulated disulphide may form within Ephrin-A5 between cysteines 62 and 102 (66 and 106 respectively in this structure).

Details

Redox score ?
85
PDB code
1shw
Structure name
ephb2 / ephrina5 complex structure
Structure deposition date
2004-02-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08543
Residue number A
62
Residue number B
102
Peptide name
Ephrin-A5

Ligandability

Cysteine 62 of Ephrin-A5

Cysteine 102 of Ephrin-A5

A redox-regulated disulphide may form within Ephrin-A5 between cysteines 53 and 164 (57 and 169 respectively in this structure).

Details

Redox score ?
85
PDB code
2x11
Structure name
crystal structure of the complete epha2 ectodomain in complex with ephrin a5 receptor binding domain
Structure deposition date
2009-12-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P52803
Residue number A
53
Residue number B
164
Peptide name
Ephrin-A5

Ligandability

Cysteine 53 of Ephrin-A5

Cysteine 164 of Ephrin-A5

A redox-regulated disulphide may form within Ephrin-A5 between cysteines 90 and 151.

Details

Redox score ?
84
PDB code
3mx0
Structure name
crystal structure of epha2 ectodomain in complex with ephrin-a5
Structure deposition date
2010-05-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P52803
Residue number A
90
Residue number B
151
Peptide name
Ephrin-A5

Ligandability

Cysteine 90 of Ephrin-A5

Cysteine 151 of Ephrin-A5

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