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Ephrin type-B receptor 2

Intramolecular
Cysteine 272 and cysteine 286 L
Cysteine 365 and cysteine 372
Cysteine 289 and cysteine 303 L
Cysteine 362 and cysteine 375 L
Cysteine 256 and cysteine 269
Cysteine 305 and cysteine 321
Cysteine 97 and cysteine 107
Cysteine 197 and cysteine 241
Cysteine 226 and cysteine 254
Cysteine 62 and cysteine 184
More...
Cysteine 107 and cysteine 184
Cysteine 372 and cysteine 375 L
Cysteine 62 and cysteine 107
Cysteine 303 and cysteine 321
Cysteine 226 and cysteine 269
Cysteine 289 and cysteine 321 L
Cysteine 303 and cysteine 305
Cysteine 254 and cysteine 269
Cysteine 256 and cysteine 286 L
Cysteine 97 and cysteine 184
Cysteine 365 and cysteine 375 L
Cysteine 272 and cysteine 303
Cysteine 272 and cysteine 289 L
Cysteine 62 and cysteine 97
Cysteine 289 and cysteine 305 L
Cysteine 362 and cysteine 372
Cysteine 226 and cysteine 256
Cysteine 256 and cysteine 272
Cysteine 254 and cysteine 256
A redox-regulated disulphide may form within Ephrin type-B receptor 2 between cysteines 272 and 286.

Details

Redox score ?
88
PDB code
7s7k
Structure name
crystal structure of the ephb2 extracellular domain
Structure deposition date
2021-09-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54763
Residue number A
272
Residue number B
286
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 272 of Ephrin type-B 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 286 of Ephrin type-B 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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Ephrin type-B receptor 2 between cysteines 365 and 372.

Details

Redox score ?
88
PDB code
7s7k
Structure name
crystal structure of the ephb2 extracellular domain
Structure deposition date
2021-09-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54763
Residue number A
365
Residue number B
372
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 365 of Ephrin type-B 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 372 of Ephrin type-B 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-B receptor 2 between cysteines 289 and 303.

Details

Redox score ?
87
PDB code
7s7k
Structure name
crystal structure of the ephb2 extracellular domain
Structure deposition date
2021-09-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54763
Residue number A
289
Residue number B
303
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 289 of Ephrin type-B 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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 303 of Ephrin type-B 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-B receptor 2 between cysteines 362 and 375.

Details

Redox score ?
87
PDB code
7s7k
Structure name
crystal structure of the ephb2 extracellular domain
Structure deposition date
2021-09-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54763
Residue number A
362
Residue number B
375
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 362 of Ephrin type-B 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 375 of Ephrin type-B 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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Ephrin type-B receptor 2 between cysteines 256 and 269.

Details

Redox score ?
86
PDB code
7s7k
Structure name
crystal structure of the ephb2 extracellular domain
Structure deposition date
2021-09-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54763
Residue number A
256
Residue number B
269
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 256 of Ephrin type-B 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 269 of Ephrin type-B 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-B receptor 2 between cysteines 305 and 321.

Details

Redox score ?
85
PDB code
7s7k
Structure name
crystal structure of the ephb2 extracellular domain
Structure deposition date
2021-09-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54763
Residue number A
305
Residue number B
321
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 305 of Ephrin type-B 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 321 of Ephrin type-B 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-B receptor 2 between cysteines 97 and 107 (505 and 515 respectively in this structure).

Details

Redox score ?
85
PDB code
1kgy
Structure name
crystal structure of the ephb2-ephrinb2 complex
Structure deposition date
2001-11-28
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54763
Residue number A
97
Residue number B
107
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 97 of Ephrin type-B 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 107 of Ephrin type-B 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-B receptor 2 between cysteines 197 and 241.

Details

Redox score ?
84
PDB code
7s7k
Structure name
crystal structure of the ephb2 extracellular domain
Structure deposition date
2021-09-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54763
Residue number A
197
Residue number B
241
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 197 of Ephrin type-B 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 241 of Ephrin type-B 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-B receptor 2 between cysteines 226 and 254.

Details

Redox score ?
83
PDB code
7s7k
Structure name
crystal structure of the ephb2 extracellular domain
Structure deposition date
2021-09-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54763
Residue number A
226
Residue number B
254
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 226 of Ephrin type-B 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 254 of Ephrin type-B 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-B receptor 2 between cysteines 62 and 184 (670 and 792 respectively in this structure).

Details

Redox score ?
79
PDB code
1kgy
Structure name
crystal structure of the ephb2-ephrinb2 complex
Structure deposition date
2001-11-28
Thiol separation (Å)
2
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54763
Residue number A
62
Residue number B
184
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 62 of Ephrin type-B 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 184 of Ephrin type-B 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-B receptor 2 between cysteines 107 and 184 (115 and 192 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
2qbx
Structure name
ephb2/snew antagonistic peptide complex
Structure deposition date
2007-06-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29323
Residue number A
107
Residue number B
184
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 107 of Ephrin type-B 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 184 of Ephrin type-B 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-B receptor 2 between cysteines 372 and 375. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
7s7k
Structure name
crystal structure of the ephb2 extracellular domain
Structure deposition date
2021-09-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
42
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54763
Residue number A
372
Residue number B
375
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 372 of Ephrin type-B 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 375 of Ephrin type-B 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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Ephrin type-B receptor 2 between cysteines 62 and 107 (70 and 115 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
2qbx
Structure name
ephb2/snew antagonistic peptide complex
Structure deposition date
2007-06-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29323
Residue number A
62
Residue number B
107
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 62 of Ephrin type-B 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 107 of Ephrin type-B 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-B receptor 2 between cysteines 303 and 321. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
7s7k
Structure name
crystal structure of the ephb2 extracellular domain
Structure deposition date
2021-09-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54763
Residue number A
303
Residue number B
321
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 303 of Ephrin type-B 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 321 of Ephrin type-B 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-B receptor 2 between cysteines 226 and 269. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
7s7k
Structure name
crystal structure of the ephb2 extracellular domain
Structure deposition date
2021-09-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54763
Residue number A
226
Residue number B
269
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 226 of Ephrin type-B 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 269 of Ephrin type-B 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-B receptor 2 between cysteines 289 and 321. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
7s7k
Structure name
crystal structure of the ephb2 extracellular domain
Structure deposition date
2021-09-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54763
Residue number A
289
Residue number B
321
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 289 of Ephrin type-B 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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 321 of Ephrin type-B 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-B receptor 2 between cysteines 303 and 305. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
7s7k
Structure name
crystal structure of the ephb2 extracellular domain
Structure deposition date
2021-09-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54763
Residue number A
303
Residue number B
305
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 303 of Ephrin type-B 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 305 of Ephrin type-B 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-B receptor 2 between cysteines 254 and 269. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
7s7k
Structure name
crystal structure of the ephb2 extracellular domain
Structure deposition date
2021-09-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54763
Residue number A
254
Residue number B
269
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 254 of Ephrin type-B 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 269 of Ephrin type-B 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-B receptor 2 between cysteines 256 and 286. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
7s7k
Structure name
crystal structure of the ephb2 extracellular domain
Structure deposition date
2021-09-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54763
Residue number A
256
Residue number B
286
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 256 of Ephrin type-B 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 286 of Ephrin type-B 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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Ephrin type-B receptor 2 between cysteines 97 and 184 (105 and 192 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
2qbx
Structure name
ephb2/snew antagonistic peptide complex
Structure deposition date
2007-06-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29323
Residue number A
97
Residue number B
184
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 97 of Ephrin type-B 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 184 of Ephrin type-B 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-B receptor 2 between cysteines 365 and 375. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
7s7k
Structure name
crystal structure of the ephb2 extracellular domain
Structure deposition date
2021-09-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54763
Residue number A
365
Residue number B
375
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 365 of Ephrin type-B 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 375 of Ephrin type-B 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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Ephrin type-B receptor 2 between cysteines 272 and 303. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
7s7k
Structure name
crystal structure of the ephb2 extracellular domain
Structure deposition date
2021-09-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54763
Residue number A
272
Residue number B
303
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 272 of Ephrin type-B 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 303 of Ephrin type-B 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-B receptor 2 between cysteines 272 and 289. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
7s7k
Structure name
crystal structure of the ephb2 extracellular domain
Structure deposition date
2021-09-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54763
Residue number A
272
Residue number B
289
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 272 of Ephrin type-B 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 289 of Ephrin type-B 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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Ephrin type-B receptor 2 between cysteines 62 and 97 (70 and 105 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
2qbx
Structure name
ephb2/snew antagonistic peptide complex
Structure deposition date
2007-06-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29323
Residue number A
62
Residue number B
97
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 62 of Ephrin type-B 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 97 of Ephrin type-B 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-B receptor 2 between cysteines 289 and 305. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
7s7k
Structure name
crystal structure of the ephb2 extracellular domain
Structure deposition date
2021-09-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54763
Residue number A
289
Residue number B
305
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 289 of Ephrin type-B 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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 305 of Ephrin type-B 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-B receptor 2 between cysteines 362 and 372. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
7s7k
Structure name
crystal structure of the ephb2 extracellular domain
Structure deposition date
2021-09-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54763
Residue number A
362
Residue number B
372
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 362 of Ephrin type-B 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 372 of Ephrin type-B 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-B receptor 2 between cysteines 226 and 256. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
7s7k
Structure name
crystal structure of the ephb2 extracellular domain
Structure deposition date
2021-09-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54763
Residue number A
226
Residue number B
256
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 226 of Ephrin type-B 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 256 of Ephrin type-B 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-B receptor 2 between cysteines 256 and 272. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
7s7k
Structure name
crystal structure of the ephb2 extracellular domain
Structure deposition date
2021-09-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54763
Residue number A
256
Residue number B
272
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 256 of Ephrin type-B 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 272 of Ephrin type-B 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-B receptor 2 between cysteines 254 and 256. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
7s7k
Structure name
crystal structure of the ephb2 extracellular domain
Structure deposition date
2021-09-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P54763
Residue number A
254
Residue number B
256
Peptide name
Ephrin type-B receptor 2

Ligandability

Cysteine 254 of Ephrin type-B 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 256 of Ephrin type-B 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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