ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Ephrin type-A receptor 2

Intermolecular
Cysteine 201 and cysteine 80 of Ephrin-A1
Intramolecular
Cysteine 276 and cysteine 290
Cysteine 366 and cysteine 379
Cysteine 369 and cysteine 376
Cysteine 293 and cysteine 307
Cysteine 105 and cysteine 115
Cysteine 262 and cysteine 273
Cysteine 309 and cysteine 325
Cysteine 201 and cysteine 247
Cysteine 230 and cysteine 260
More...
Cysteine 70 and cysteine 188
Cysteine 369 and cysteine 379
Cysteine 230 and cysteine 273
Cysteine 70 and cysteine 115
Cysteine 260 and cysteine 273
Cysteine 276 and cysteine 307
Cysteine 307 and cysteine 309
Cysteine 262 and cysteine 290
Cysteine 307 and cysteine 325
Cysteine 276 and cysteine 293
Cysteine 273 and cysteine 276
Cysteine 262 and cysteine 276
Cysteine 366 and cysteine 369
Cysteine 105 and cysteine 188
Cysteine 293 and cysteine 325
Cysteine 273 and cysteine 290
Cysteine 115 and cysteine 188
Cysteine 70 and cysteine 105
Cysteine 293 and cysteine 309
Cysteine 290 and cysteine 293
Cysteine 290 and cysteine 307
Cysteine 260 and cysteine 262
Cysteine 230 and cysteine 262
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 type-A receptor 2 between cysteines 276 and 290.

Details

Redox score ?
88
PDB code
2x10
Structure name
crystal structure of the complete epha2 ectodomain
Structure deposition date
2009-12-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29317
Residue number A
276
Residue number B
290
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 276 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 290 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 366 and 379.

Details

Redox score ?
87
PDB code
3mx0
Structure name
crystal structure of epha2 ectodomain in complex with ephrin-a5
Structure deposition date
2010-05-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29317
Residue number A
366
Residue number B
379
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 366 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 379 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 369 and 376.

Details

Redox score ?
87
PDB code
3mx0
Structure name
crystal structure of epha2 ectodomain in complex with ephrin-a5
Structure deposition date
2010-05-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
40
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29317
Residue number A
369
Residue number B
376
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 369 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 376 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 293 and 307.

Details

Redox score ?
86
PDB code
3mx0
Structure name
crystal structure of epha2 ectodomain in complex with ephrin-a5
Structure deposition date
2010-05-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29317
Residue number A
293
Residue number B
307
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 293 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 307 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 105 and 115.

Details

Redox score ?
86
PDB code
3mx0
Structure name
crystal structure of epha2 ectodomain in complex with ephrin-a5
Structure deposition date
2010-05-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29317
Residue number A
105
Residue number B
115
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 105 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 115 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 262 and 273.

Details

Redox score ?
86
PDB code
3mx0
Structure name
crystal structure of epha2 ectodomain in complex with ephrin-a5
Structure deposition date
2010-05-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29317
Residue number A
262
Residue number B
273
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 262 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 273 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 309 and 325.

Details

Redox score ?
85
PDB code
3mx0
Structure name
crystal structure of epha2 ectodomain in complex with ephrin-a5
Structure deposition date
2010-05-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29317
Residue number A
309
Residue number B
325
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 309 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 325 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 201 and 247.

Details

Redox score ?
84
PDB code
3mx0
Structure name
crystal structure of epha2 ectodomain in complex with ephrin-a5
Structure deposition date
2010-05-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29317
Residue number A
201
Residue number B
247
Peptide name
Ephrin type-A receptor 2

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 247 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 230 and 260.

Details

Redox score ?
83
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 ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29317
Residue number A
230
Residue number B
260
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 230 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 260 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 70 and 188.

Details

Redox score ?
79
PDB code
3mx0
Structure name
crystal structure of epha2 ectodomain in complex with ephrin-a5
Structure deposition date
2010-05-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29317
Residue number A
70
Residue number B
188
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 70 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 188 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 369 and 379 (376 and 379 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
2x10
Structure name
crystal structure of the complete epha2 ectodomain
Structure deposition date
2009-12-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
nan
Peptide accession
P29317
Residue number A
369
Residue number B
379
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 369 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 379 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 230 and 273. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
3fl7
Structure name
crystal structure of the human ephrin a2 ectodomain
Structure deposition date
2008-12-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8N3Z2
Residue number A
230
Residue number B
273
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 230 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 273 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 70 and 115. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
3mx0
Structure name
crystal structure of epha2 ectodomain in complex with ephrin-a5
Structure deposition date
2010-05-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29317
Residue number A
70
Residue number B
115
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 70 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 115 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 260 and 273. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
3fl7
Structure name
crystal structure of the human ephrin a2 ectodomain
Structure deposition date
2008-12-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8N3Z2
Residue number A
260
Residue number B
273
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 260 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 273 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 276 and 307. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
3fl7
Structure name
crystal structure of the human ephrin a2 ectodomain
Structure deposition date
2008-12-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8N3Z2
Residue number A
276
Residue number B
307
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 276 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 307 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 307 and 309. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
3mx0
Structure name
crystal structure of epha2 ectodomain in complex with ephrin-a5
Structure deposition date
2010-05-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29317
Residue number A
307
Residue number B
309
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 307 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 309 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 262 and 290. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
3fl7
Structure name
crystal structure of the human ephrin a2 ectodomain
Structure deposition date
2008-12-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8N3Z2
Residue number A
262
Residue number B
290
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 262 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 290 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 307 and 325. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
3fl7
Structure name
crystal structure of the human ephrin a2 ectodomain
Structure deposition date
2008-12-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8N3Z2
Residue number A
307
Residue number B
325
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 307 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 325 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 276 and 293. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
3fl7
Structure name
crystal structure of the human ephrin a2 ectodomain
Structure deposition date
2008-12-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8N3Z2
Residue number A
276
Residue number B
293
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 276 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 293 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 273 and 276. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
3mx0
Structure name
crystal structure of epha2 ectodomain in complex with ephrin-a5
Structure deposition date
2010-05-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29317
Residue number A
273
Residue number B
276
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 273 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 276 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 262 and 276. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
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)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29317
Residue number A
262
Residue number B
276
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 262 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 276 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 366 and 369. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
2x11
Structure name
crystal structure of the complete epha2 ectodomain in complex with ephrin a5 receptor binding domain
Structure deposition date
2009-12-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29317
Residue number A
366
Residue number B
369
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 366 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 369 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 105 and 188. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
6b9l
Structure name
crystal structure of epha2 with peptide 135e2
Structure deposition date
2017-10-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29317
Residue number A
105
Residue number B
188
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 105 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 188 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 293 and 325. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
3fl7
Structure name
crystal structure of the human ephrin a2 ectodomain
Structure deposition date
2008-12-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8N3Z2
Residue number A
293
Residue number B
325
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 293 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 325 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 273 and 290. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
2x11
Structure name
crystal structure of the complete epha2 ectodomain in complex with ephrin a5 receptor binding domain
Structure deposition date
2009-12-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29317
Residue number A
273
Residue number B
290
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 273 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 290 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 115 and 188. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
7b7n
Structure name
human herpesvirus-8 gh/gl in complex with epha2
Structure deposition date
2020-12-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29317
Residue number A
115
Residue number B
188
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 115 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 188 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 70 and 105. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
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)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29317
Residue number A
70
Residue number B
105
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 70 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 105 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 293 and 309. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
3mx0
Structure name
crystal structure of epha2 ectodomain in complex with ephrin-a5
Structure deposition date
2010-05-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29317
Residue number A
293
Residue number B
309
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 293 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 309 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 290 and 293. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
3fl7
Structure name
crystal structure of the human ephrin a2 ectodomain
Structure deposition date
2008-12-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8N3Z2
Residue number A
290
Residue number B
293
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 290 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 293 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 290 and 307. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
3mx0
Structure name
crystal structure of epha2 ectodomain in complex with ephrin-a5
Structure deposition date
2010-05-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29317
Residue number A
290
Residue number B
307
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 290 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 307 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 260 and 262. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
3fl7
Structure name
crystal structure of the human ephrin a2 ectodomain
Structure deposition date
2008-12-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8N3Z2
Residue number A
260
Residue number B
262
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 260 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 262 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.

A redox-regulated disulphide may form within Ephrin type-A receptor 2 between cysteines 230 and 262. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
3fl7
Structure name
crystal structure of the human ephrin a2 ectodomain
Structure deposition date
2008-12-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8N3Z2
Residue number A
230
Residue number B
262
Peptide name
Ephrin type-A receptor 2

Ligandability

Cysteine 230 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 262 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.

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