ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Ephrin type-A receptor 4

Intermolecular
Cysteine 108 and cysteine 108
Cysteine 118 and cysteine 108
Intramolecular
Cysteine 276 and cysteine 290
Cysteine 366 and cysteine 380
Cysteine 369 and cysteine 377
Cysteine 233 and cysteine 260
Cysteine 293 and cysteine 307
Cysteine 262 and cysteine 273
Cysteine 309 and cysteine 325
Cysteine 204 and cysteine 247
More...
Cysteine 73 and cysteine 191
Cysteine 233 and cysteine 262
Cysteine 273 and cysteine 276
Cysteine 260 and cysteine 273
Cysteine 276 and cysteine 307
Cysteine 366 and cysteine 377
Cysteine 233 and cysteine 273
Cysteine 260 and cysteine 262
Cysteine 307 and cysteine 325
Cysteine 73 and cysteine 118
Cysteine 262 and cysteine 290
Cysteine 73 and cysteine 108
Cysteine 307 and cysteine 309
Cysteine 293 and cysteine 325
Cysteine 262 and cysteine 276
Cysteine 377 and cysteine 380
Cysteine 369 and cysteine 380
Cysteine 293 and cysteine 309
Cysteine 118 and cysteine 191
Cysteine 273 and cysteine 290
Cysteine 108 and cysteine 191
Cysteine 276 and cysteine 293
Cysteine 290 and cysteine 293
Cysteine 290 and cysteine 307
Cysteine 366 and cysteine 369
A redox-regulated disulphide may form between two units of Ephrin type-A receptor 4 at cysteines 108 and 108. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
4m4r
Structure name
epha4 ectodomain complex with ephrin a5
Structure deposition date
2013-08-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide A name
Ephrin type-A receptor 4
Peptide B name
Ephrin type-A receptor 4
Peptide A accession
P54764
Peptide B accession
P54764
Peptide A residue number
108
Peptide B residue number
108

Ligandability

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 between two units of Ephrin type-A receptor 4 at cysteines 118 and 108. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
4m4r
Structure name
epha4 ectodomain complex with ephrin a5
Structure deposition date
2013-08-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide A name
Ephrin type-A receptor 4
Peptide B name
Ephrin type-A receptor 4
Peptide A accession
P54764
Peptide B accession
P54764
Peptide A residue number
118
Peptide B residue number
108

Ligandability

Cysteine 118 of Ephrin type-A 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 108 of Ephrin type-A 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-A receptor 4 between cysteines 276 and 290.

Details

Redox score ?
88
PDB code
4bk5
Structure name
crystal structure of the human epha4 ectodomain in complex with human ephrin a5 (amine-methylated sample)
Structure deposition date
2013-04-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
276
Residue number B
290
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 276 of Ephrin type-A 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 290 of Ephrin type-A 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-A receptor 4 between cysteines 366 and 380.

Details

Redox score ?
87
PDB code
4bkf
Structure name
crystal structure of the human epha4 ectodomain in complex with human ephrinb3
Structure deposition date
2013-04-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
366
Residue number B
380
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 366 of Ephrin type-A 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 380 of Ephrin type-A 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-A receptor 4 between cysteines 369 and 377.

Details

Redox score ?
86
PDB code
4bkf
Structure name
crystal structure of the human epha4 ectodomain in complex with human ephrinb3
Structure deposition date
2013-04-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
369
Residue number B
377
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 369 of Ephrin type-A 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 377 of Ephrin type-A 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-A receptor 4 between cysteines 233 and 260.

Details

Redox score ?
86
PDB code
4bkf
Structure name
crystal structure of the human epha4 ectodomain in complex with human ephrinb3
Structure deposition date
2013-04-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
233
Residue number B
260
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 233 of Ephrin type-A 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 260 of Ephrin type-A 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-A receptor 4 between cysteines 293 and 307.

Details

Redox score ?
86
PDB code
4bk5
Structure name
crystal structure of the human epha4 ectodomain in complex with human ephrin a5 (amine-methylated sample)
Structure deposition date
2013-04-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
293
Residue number B
307
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 293 of Ephrin type-A 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 307 of Ephrin type-A 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-A receptor 4 between cysteines 262 and 273.

Details

Redox score ?
85
PDB code
4bka
Structure name
crystal structure of the human epha4 ectodomain in complex with human ephrin a5
Structure deposition date
2013-04-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
262
Residue number B
273
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 262 of Ephrin type-A 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 273 of Ephrin type-A 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-A receptor 4 between cysteines 309 and 325.

Details

Redox score ?
85
PDB code
4bk5
Structure name
crystal structure of the human epha4 ectodomain in complex with human ephrin a5 (amine-methylated sample)
Structure deposition date
2013-04-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
309
Residue number B
325
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 309 of Ephrin type-A 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 325 of Ephrin type-A 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-A receptor 4 between cysteines 204 and 247.

Details

Redox score ?
84
PDB code
4bka
Structure name
crystal structure of the human epha4 ectodomain in complex with human ephrin a5
Structure deposition date
2013-04-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
204
Residue number B
247
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 204 of Ephrin type-A 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 247 of Ephrin type-A 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-A receptor 4 between cysteines 73 and 191.

Details

Redox score ?
78
PDB code
4bkf
Structure name
crystal structure of the human epha4 ectodomain in complex with human ephrinb3
Structure deposition date
2013-04-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
73
Residue number B
191
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 73 of Ephrin type-A 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 191 of Ephrin type-A 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-A receptor 4 between cysteines 233 and 262. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
4bka
Structure name
crystal structure of the human epha4 ectodomain in complex with human ephrin a5
Structure deposition date
2013-04-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
233
Residue number B
262
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 233 of Ephrin type-A 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 262 of Ephrin type-A 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-A receptor 4 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 ?
51
PDB code
4bk4
Structure name
crystal structure of the human epha4 ectodomain
Structure deposition date
2013-04-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
273
Residue number B
276
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 273 of Ephrin type-A 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 276 of Ephrin type-A 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-A receptor 4 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 ?
50
PDB code
4m4r
Structure name
epha4 ectodomain complex with ephrin a5
Structure deposition date
2013-08-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
260
Residue number B
273
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 260 of Ephrin type-A 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 273 of Ephrin type-A 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-A receptor 4 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 ?
48
PDB code
4bk4
Structure name
crystal structure of the human epha4 ectodomain
Structure deposition date
2013-04-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
276
Residue number B
307
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 276 of Ephrin type-A 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 307 of Ephrin type-A 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-A receptor 4 between cysteines 366 and 377. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
4m4r
Structure name
epha4 ectodomain complex with ephrin a5
Structure deposition date
2013-08-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
366
Residue number B
377
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 366 of Ephrin type-A 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 377 of Ephrin type-A 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-A receptor 4 between cysteines 233 and 273. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
4m4r
Structure name
epha4 ectodomain complex with ephrin a5
Structure deposition date
2013-08-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
233
Residue number B
273
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 233 of Ephrin type-A 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 273 of Ephrin type-A 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-A receptor 4 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 ?
47
PDB code
4bk4
Structure name
crystal structure of the human epha4 ectodomain
Structure deposition date
2013-04-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
260
Residue number B
262
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 260 of Ephrin type-A 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 262 of Ephrin type-A 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-A receptor 4 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
4bkf
Structure name
crystal structure of the human epha4 ectodomain in complex with human ephrinb3
Structure deposition date
2013-04-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
307
Residue number B
325
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 307 of Ephrin type-A 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 325 of Ephrin type-A 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-A receptor 4 between cysteines 73 and 118. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
4bk4
Structure name
crystal structure of the human epha4 ectodomain
Structure deposition date
2013-04-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
73
Residue number B
118
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 73 of Ephrin type-A 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 118 of Ephrin type-A 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-A receptor 4 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 ?
46
PDB code
4bk4
Structure name
crystal structure of the human epha4 ectodomain
Structure deposition date
2013-04-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
262
Residue number B
290
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 262 of Ephrin type-A 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 290 of Ephrin type-A 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-A receptor 4 between cysteines 73 and 108. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
7ofv
Structure name
nmr-guided design of potent and selective epha4 agonistic ligands
Structure deposition date
2021-05-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
73
Residue number B
108
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 73 of Ephrin type-A 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 108 of Ephrin type-A 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-A receptor 4 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 ?
46
PDB code
4bk4
Structure name
crystal structure of the human epha4 ectodomain
Structure deposition date
2013-04-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
307
Residue number B
309
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 307 of Ephrin type-A 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 309 of Ephrin type-A 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-A receptor 4 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 ?
46
PDB code
4bka
Structure name
crystal structure of the human epha4 ectodomain in complex with human ephrin a5
Structure deposition date
2013-04-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
293
Residue number B
325
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 293 of Ephrin type-A 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 325 of Ephrin type-A 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-A receptor 4 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
4m4r
Structure name
epha4 ectodomain complex with ephrin a5
Structure deposition date
2013-08-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
262
Residue number B
276
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 262 of Ephrin type-A 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 276 of Ephrin type-A 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-A receptor 4 between cysteines 377 and 380. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
4m4r
Structure name
epha4 ectodomain complex with ephrin a5
Structure deposition date
2013-08-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
42
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
377
Residue number B
380
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 377 of Ephrin type-A 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 380 of Ephrin type-A 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-A receptor 4 between cysteines 369 and 380. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
4m4r
Structure name
epha4 ectodomain complex with ephrin a5
Structure deposition date
2013-08-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
43
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
369
Residue number B
380
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 369 of Ephrin type-A 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 380 of Ephrin type-A 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-A receptor 4 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 ?
44
PDB code
4m4r
Structure name
epha4 ectodomain complex with ephrin a5
Structure deposition date
2013-08-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
293
Residue number B
309
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 293 of Ephrin type-A 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 309 of Ephrin type-A 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-A receptor 4 between cysteines 118 and 191. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
2wo2
Structure name
crystal structure of the epha4-ephrinb2 complex
Structure deposition date
2009-07-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
118
Residue number B
191
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 118 of Ephrin type-A 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 191 of Ephrin type-A 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-A receptor 4 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
4m4r
Structure name
epha4 ectodomain complex with ephrin a5
Structure deposition date
2013-08-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
273
Residue number B
290
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 273 of Ephrin type-A 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 290 of Ephrin type-A 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-A receptor 4 between cysteines 108 and 191. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
4bk5
Structure name
crystal structure of the human epha4 ectodomain in complex with human ephrin a5 (amine-methylated sample)
Structure deposition date
2013-04-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
108
Residue number B
191
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 108 of Ephrin type-A 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 191 of Ephrin type-A 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-A receptor 4 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 ?
43
PDB code
4bka
Structure name
crystal structure of the human epha4 ectodomain in complex with human ephrin a5
Structure deposition date
2013-04-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
276
Residue number B
293
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 276 of Ephrin type-A 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 293 of Ephrin type-A 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-A receptor 4 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 ?
43
PDB code
4m4p
Structure name
crystal structure of epha4 ectodomain
Structure deposition date
2013-08-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
290
Residue number B
293
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 290 of Ephrin type-A 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 293 of Ephrin type-A 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-A receptor 4 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
4bk4
Structure name
crystal structure of the human epha4 ectodomain
Structure deposition date
2013-04-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
290
Residue number B
307
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 290 of Ephrin type-A 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 307 of Ephrin type-A 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-A receptor 4 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 ?
42
PDB code
4bk5
Structure name
crystal structure of the human epha4 ectodomain in complex with human ephrin a5 (amine-methylated sample)
Structure deposition date
2013-04-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54764
Residue number A
366
Residue number B
369
Peptide name
Ephrin type-A receptor 4

Ligandability

Cysteine 366 of Ephrin type-A 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 369 of Ephrin type-A 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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