ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Ephrin type-B receptor 4

Intramolecular
Cysteine 97 and cysteine 107
Cysteine 61 and cysteine 184
Cysteine 107 and cysteine 184
Cysteine 61 and cysteine 107
Cysteine 97 and cysteine 184
Cysteine 61 and cysteine 97
A redox-regulated disulphide may form within Ephrin type-B receptor 4 between cysteines 97 and 107.

Details

Redox score ?
86
PDB code
2bba
Structure name
crystal structure and thermodynamic characterization of the ephb4 receptor in complex with an ephrin-b2 antagonist peptide reveals the determinants for receptor specificity
Structure deposition date
2005-10-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54760
Residue number A
97
Residue number B
107
Peptide name
Ephrin type-B receptor 4

Ligandability

Cysteine 97 of Ephrin type-B receptor 4

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 107 of Ephrin type-B receptor 4

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 4 between cysteines 61 and 184.

Details

Redox score ?
77
PDB code
2bba
Structure name
crystal structure and thermodynamic characterization of the ephb4 receptor in complex with an ephrin-b2 antagonist peptide reveals the determinants for receptor specificity
Structure deposition date
2005-10-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
99
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54760
Residue number A
61
Residue number B
184
Peptide name
Ephrin type-B receptor 4

Ligandability

Cysteine 61 of Ephrin type-B receptor 4

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 184 of Ephrin type-B receptor 4

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 4 between cysteines 107 and 184. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
2hle
Structure name
structural and biophysical characterization of the ephb4-ephrinb2 protein protein interaction and receptor specificity
Structure deposition date
2006-07-06
Thiol separation (Å)
7
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54760
Residue number A
107
Residue number B
184
Peptide name
Ephrin type-B receptor 4

Ligandability

Cysteine 107 of Ephrin type-B receptor 4

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 184 of Ephrin type-B receptor 4

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 4 between cysteines 61 and 107. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
2bba
Structure name
crystal structure and thermodynamic characterization of the ephb4 receptor in complex with an ephrin-b2 antagonist peptide reveals the determinants for receptor specificity
Structure deposition date
2005-10-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54760
Residue number A
61
Residue number B
107
Peptide name
Ephrin type-B receptor 4

Ligandability

Cysteine 61 of Ephrin type-B receptor 4

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 107 of Ephrin type-B receptor 4

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 4 between cysteines 97 and 184. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
2hle
Structure name
structural and biophysical characterization of the ephb4-ephrinb2 protein protein interaction and receptor specificity
Structure deposition date
2006-07-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54760
Residue number A
97
Residue number B
184
Peptide name
Ephrin type-B receptor 4

Ligandability

Cysteine 97 of Ephrin type-B receptor 4

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 184 of Ephrin type-B receptor 4

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 4 between cysteines 61 and 97. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
2bba
Structure name
crystal structure and thermodynamic characterization of the ephb4 receptor in complex with an ephrin-b2 antagonist peptide reveals the determinants for receptor specificity
Structure deposition date
2005-10-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54760
Residue number A
61
Residue number B
97
Peptide name
Ephrin type-B receptor 4

Ligandability

Cysteine 61 of Ephrin type-B receptor 4

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 97 of Ephrin type-B receptor 4

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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