ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Ephrin type-A receptor 5

Intramolecular
Cysteine 137 and cysteine 147
Cysteine 102 and cysteine 220
Cysteine 147 and cysteine 220
Cysteine 102 and cysteine 147
Cysteine 137 and cysteine 220
Cysteine 102 and cysteine 137
A redox-regulated disulphide may form within Ephrin type-A receptor 5 between cysteines 137 and 147.

Details

Redox score ?
86
PDB code
4et7
Structure name
crystal structure of eph receptor 5
Structure deposition date
2012-04-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54756
Residue number A
137
Residue number B
147
Peptide name
Ephrin type-A receptor 5

Ligandability

Cysteine 137 of Ephrin type-A receptor 5

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 147 of Ephrin type-A receptor 5

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 Ephrin type-A receptor 5 between cysteines 102 and 220.

Details

Redox score ?
78
PDB code
4et7
Structure name
crystal structure of eph receptor 5
Structure deposition date
2012-04-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54756
Residue number A
102
Residue number B
220
Peptide name
Ephrin type-A receptor 5

Ligandability

Cysteine 102 of Ephrin type-A receptor 5

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 220 of Ephrin type-A receptor 5

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 Ephrin type-A receptor 5 between cysteines 147 and 220. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
4et7
Structure name
crystal structure of eph receptor 5
Structure deposition date
2012-04-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54756
Residue number A
147
Residue number B
220
Peptide name
Ephrin type-A receptor 5

Ligandability

Cysteine 147 of Ephrin type-A receptor 5

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 220 of Ephrin type-A receptor 5

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 Ephrin type-A receptor 5 between cysteines 102 and 147. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
4et7
Structure name
crystal structure of eph receptor 5
Structure deposition date
2012-04-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54756
Residue number A
102
Residue number B
147
Peptide name
Ephrin type-A receptor 5

Ligandability

Cysteine 102 of Ephrin type-A receptor 5

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 147 of Ephrin type-A receptor 5

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 Ephrin type-A receptor 5 between cysteines 137 and 220. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
4et7
Structure name
crystal structure of eph receptor 5
Structure deposition date
2012-04-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54756
Residue number A
137
Residue number B
220
Peptide name
Ephrin type-A receptor 5

Ligandability

Cysteine 137 of Ephrin type-A receptor 5

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 220 of Ephrin type-A receptor 5

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 Ephrin type-A receptor 5 between cysteines 102 and 137. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
4et7
Structure name
crystal structure of eph receptor 5
Structure deposition date
2012-04-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54756
Residue number A
102
Residue number B
137
Peptide name
Ephrin type-A receptor 5

Ligandability

Cysteine 102 of Ephrin type-A receptor 5

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 137 of Ephrin type-A receptor 5

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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