ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Ephrin-A1

Intermolecular
Cysteine 201 of Ephrin type-A receptor 2 and cysteine 80
Intramolecular
Cysteine 80 and cysteine 140
Cysteine 51 and cysteine 92
A redox-regulated disulphide may form between cysteine 201 of Ephrin type-A receptor 2 and cysteine 80 of Ephrin-A1 (174 and 80 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
3hei
Structure name
ligand recognition by a-class eph receptors: crystal structures of the epha2 ligand-binding domain and the epha2/ephrin-a1 complex
Structure deposition date
2009-05-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
nan
Peptide A name
Ephrin type-A receptor 2
Peptide B name
Ephrin-A1
Peptide A accession
P29317
Peptide B accession
P20827
Peptide A residue number
201
Peptide B residue number
80

Ligandability

Cysteine 201 of Ephrin type-A receptor 2

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 80 of Ephrin-A1

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-A1 between cysteines 80 and 140.

Details

Redox score ?
84
PDB code
3mbw
Structure name
crystal structure of the human ephrin a2 lbd and crd domains in complex with ephrin a1
Structure deposition date
2010-03-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20827
Residue number A
80
Residue number B
140
Peptide name
Ephrin-A1

Ligandability

Cysteine 80 of Ephrin-A1

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 140 of Ephrin-A1

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-A1 between cysteines 51 and 92.

Details

Redox score ?
84
PDB code
3mbw
Structure name
crystal structure of the human ephrin a2 lbd and crd domains in complex with ephrin a1
Structure deposition date
2010-03-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20827
Residue number A
51
Residue number B
92
Peptide name
Ephrin-A1

Ligandability

Cysteine 51 of Ephrin-A1

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 92 of Ephrin-A1

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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