ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Ephrin type-A receptor 3

Intramolecular
Cysteine 106 and cysteine 116
Cysteine 71 and cysteine 189
Cysteine 116 and cysteine 189
Cysteine 71 and cysteine 116
Cysteine 106 and cysteine 189
Cysteine 71 and cysteine 106
A redox-regulated disulphide may form within Ephrin type-A receptor 3 between cysteines 106 and 116.

Details

Redox score ?
86
PDB code
4l0p
Structure name
structure of the human epha3 receptor ligand binding domain complexed with ephrin-a5
Structure deposition date
2013-05-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29320
Residue number A
106
Residue number B
116
Peptide name
Ephrin type-A receptor 3

Ligandability

Cysteine 106 of Ephrin type-A receptor 3

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 116 of Ephrin type-A receptor 3

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 3 between cysteines 71 and 189.

Details

Redox score ?
78
PDB code
4l0p
Structure name
structure of the human epha3 receptor ligand binding domain complexed with ephrin-a5
Structure deposition date
2013-05-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
95
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29320
Residue number A
71
Residue number B
189
Peptide name
Ephrin type-A receptor 3

Ligandability

Cysteine 71 of Ephrin type-A receptor 3

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 189 of Ephrin type-A receptor 3

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 3 between cysteines 116 and 189. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
4l0p
Structure name
structure of the human epha3 receptor ligand binding domain complexed with ephrin-a5
Structure deposition date
2013-05-31
Thiol separation (Å)
7
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29320
Residue number A
116
Residue number B
189
Peptide name
Ephrin type-A receptor 3

Ligandability

Cysteine 116 of Ephrin type-A receptor 3

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 189 of Ephrin type-A receptor 3

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 3 between cysteines 71 and 116. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
4l0p
Structure name
structure of the human epha3 receptor ligand binding domain complexed with ephrin-a5
Structure deposition date
2013-05-31
Thiol separation (Å)
7
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29320
Residue number A
71
Residue number B
116
Peptide name
Ephrin type-A receptor 3

Ligandability

Cysteine 71 of Ephrin type-A receptor 3

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 116 of Ephrin type-A receptor 3

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 3 between cysteines 106 and 189. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
4l0p
Structure name
structure of the human epha3 receptor ligand binding domain complexed with ephrin-a5
Structure deposition date
2013-05-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29320
Residue number A
106
Residue number B
189
Peptide name
Ephrin type-A receptor 3

Ligandability

Cysteine 106 of Ephrin type-A receptor 3

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 189 of Ephrin type-A receptor 3

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 3 between cysteines 71 and 106. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
4l0p
Structure name
structure of the human epha3 receptor ligand binding domain complexed with ephrin-a5
Structure deposition date
2013-05-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29320
Residue number A
71
Residue number B
106
Peptide name
Ephrin type-A receptor 3

Ligandability

Cysteine 71 of Ephrin type-A receptor 3

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 106 of Ephrin type-A receptor 3

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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