ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Ephrin type-B receptor 3

Intramolecular
Cysteine 116 and cysteine 126
Cysteine 81 and cysteine 199
Cysteine 126 and cysteine 199
Cysteine 81 and cysteine 126
Cysteine 116 and cysteine 199
Cysteine 81 and cysteine 116
A redox-regulated disulphide may form within Ephrin type-B receptor 3 between cysteines 116 and 126.

Details

Redox score ?
87
PDB code
3p1i
Structure name
ligand binding domain of human ephrin type-b receptor 3
Structure deposition date
2010-09-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54753
Residue number A
116
Residue number B
126
Peptide name
Ephrin type-B receptor 3

Ligandability

Cysteine 116 of Ephrin type-B 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 126 of Ephrin type-B 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-B receptor 3 between cysteines 81 and 199.

Details

Redox score ?
79
PDB code
3p1i
Structure name
ligand binding domain of human ephrin type-b receptor 3
Structure deposition date
2010-09-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
89
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54753
Residue number A
81
Residue number B
199
Peptide name
Ephrin type-B receptor 3

Ligandability

Cysteine 81 of Ephrin type-B 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 199 of Ephrin type-B 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-B receptor 3 between cysteines 126 and 199. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
3p1i
Structure name
ligand binding domain of human ephrin type-b receptor 3
Structure deposition date
2010-09-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54753
Residue number A
126
Residue number B
199
Peptide name
Ephrin type-B receptor 3

Ligandability

Cysteine 126 of Ephrin type-B 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 199 of Ephrin type-B 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-B receptor 3 between cysteines 81 and 126. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
3p1i
Structure name
ligand binding domain of human ephrin type-b receptor 3
Structure deposition date
2010-09-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54753
Residue number A
81
Residue number B
126
Peptide name
Ephrin type-B receptor 3

Ligandability

Cysteine 81 of Ephrin type-B 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 126 of Ephrin type-B 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-B receptor 3 between cysteines 116 and 199. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
3p1i
Structure name
ligand binding domain of human ephrin type-b receptor 3
Structure deposition date
2010-09-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54753
Residue number A
116
Residue number B
199
Peptide name
Ephrin type-B receptor 3

Ligandability

Cysteine 116 of Ephrin type-B 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 199 of Ephrin type-B 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-B receptor 3 between cysteines 81 and 116. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
3p1i
Structure name
ligand binding domain of human ephrin type-b receptor 3
Structure deposition date
2010-09-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54753
Residue number A
81
Residue number B
116
Peptide name
Ephrin type-B receptor 3

Ligandability

Cysteine 81 of Ephrin type-B 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-B 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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