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EPH receptor B6

Intramolecular
Cysteine 318 and cysteine 332
Cysteine 411 and cysteine 425
Cysteine 408 and cysteine 428
Cysteine 114 and cysteine 124
Cysteine 302 and cysteine 315
Cysteine 335 and cysteine 349
Cysteine 351 and cysteine 367
Cysteine 233 and cysteine 287
Cysteine 263 and cysteine 300
Cysteine 75 and cysteine 220
More...
Cysteine 318 and cysteine 349
Cysteine 408 and cysteine 411
Cysteine 302 and cysteine 332
Cysteine 263 and cysteine 315
Cysteine 75 and cysteine 124
Cysteine 300 and cysteine 315
Cysteine 349 and cysteine 367
Cysteine 318 and cysteine 335
Cysteine 124 and cysteine 220
Cysteine 335 and cysteine 367
Cysteine 114 and cysteine 220
Cysteine 411 and cysteine 428
Cysteine 315 and cysteine 332
Cysteine 349 and cysteine 351
Cysteine 75 and cysteine 114
Cysteine 332 and cysteine 349
Cysteine 302 and cysteine 318
Cysteine 408 and cysteine 425
Cysteine 300 and cysteine 302
A redox-regulated disulphide may form within EPH receptor B6 between cysteines 318 and 332 (286 and 300 respectively in this structure).

Details

Redox score ?
88
PDB code
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
318
Residue number B
332
Peptide name
EPH receptor B6

Ligandability

Cysteine 318 of EPH receptor B6

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 332 of EPH receptor B6

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 EPH receptor B6 between cysteines 411 and 425 (379 and 393 respectively in this structure).

Details

Redox score ?
88
PDB code
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
411
Residue number B
425
Peptide name
EPH receptor B6

Ligandability

Cysteine 411 of EPH receptor B6

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 425 of EPH receptor B6

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 EPH receptor B6 between cysteines 408 and 428 (376 and 396 respectively in this structure).

Details

Redox score ?
87
PDB code
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
408
Residue number B
428
Peptide name
EPH receptor B6

Ligandability

Cysteine 408 of EPH receptor B6

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 428 of EPH receptor B6

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 EPH receptor B6 between cysteines 114 and 124 (82 and 92 respectively in this structure).

Details

Redox score ?
87
PDB code
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
114
Residue number B
124
Peptide name
EPH receptor B6

Ligandability

Cysteine 114 of EPH receptor B6

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 124 of EPH receptor B6

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 EPH receptor B6 between cysteines 302 and 315 (270 and 283 respectively in this structure).

Details

Redox score ?
86
PDB code
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
302
Residue number B
315
Peptide name
EPH receptor B6

Ligandability

Cysteine 302 of EPH receptor B6

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 315 of EPH receptor B6

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 EPH receptor B6 between cysteines 335 and 349 (303 and 317 respectively in this structure).

Details

Redox score ?
86
PDB code
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
335
Residue number B
349
Peptide name
EPH receptor B6

Ligandability

Cysteine 335 of EPH receptor B6

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 349 of EPH receptor B6

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 EPH receptor B6 between cysteines 351 and 367 (319 and 335 respectively in this structure).

Details

Redox score ?
85
PDB code
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
351
Residue number B
367
Peptide name
EPH receptor B6

Ligandability

Cysteine 351 of EPH receptor B6

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 367 of EPH receptor B6

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 EPH receptor B6 between cysteines 233 and 287 (201 and 255 respectively in this structure).

Details

Redox score ?
84
PDB code
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
233
Residue number B
287
Peptide name
EPH receptor B6

Ligandability

Cysteine 233 of EPH receptor B6

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 287 of EPH receptor B6

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 EPH receptor B6 between cysteines 263 and 300 (231 and 268 respectively in this structure).

Details

Redox score ?
83
PDB code
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
263
Residue number B
300
Peptide name
EPH receptor B6

Ligandability

Cysteine 263 of EPH receptor B6

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 300 of EPH receptor B6

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 EPH receptor B6 between cysteines 75 and 220 (43 and 188 respectively in this structure).

Details

Redox score ?
78
PDB code
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
75
Residue number B
220
Peptide name
EPH receptor B6

Ligandability

Cysteine 75 of EPH receptor B6

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 220 of EPH receptor B6

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 EPH receptor B6 between cysteines 318 and 349 (286 and 317 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
318
Residue number B
349
Peptide name
EPH receptor B6

Ligandability

Cysteine 318 of EPH receptor B6

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 349 of EPH receptor B6

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 EPH receptor B6 between cysteines 408 and 411 (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 ?
48
PDB code
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
408
Residue number B
411
Peptide name
EPH receptor B6

Ligandability

Cysteine 408 of EPH receptor B6

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 411 of EPH receptor B6

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 EPH receptor B6 between cysteines 302 and 332 (270 and 300 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
302
Residue number B
332
Peptide name
EPH receptor B6

Ligandability

Cysteine 302 of EPH receptor B6

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 332 of EPH receptor B6

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 EPH receptor B6 between cysteines 263 and 315 (231 and 283 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
263
Residue number B
315
Peptide name
EPH receptor B6

Ligandability

Cysteine 263 of EPH receptor B6

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 315 of EPH receptor B6

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 EPH receptor B6 between cysteines 75 and 124 (43 and 92 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
75
Residue number B
124
Peptide name
EPH receptor B6

Ligandability

Cysteine 75 of EPH receptor B6

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 124 of EPH receptor B6

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 EPH receptor B6 between cysteines 300 and 315 (268 and 283 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
300
Residue number B
315
Peptide name
EPH receptor B6

Ligandability

Cysteine 300 of EPH receptor B6

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 315 of EPH receptor B6

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 EPH receptor B6 between cysteines 349 and 367 (317 and 335 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
349
Residue number B
367
Peptide name
EPH receptor B6

Ligandability

Cysteine 349 of EPH receptor B6

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 367 of EPH receptor B6

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 EPH receptor B6 between cysteines 318 and 335 (286 and 303 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
318
Residue number B
335
Peptide name
EPH receptor B6

Ligandability

Cysteine 318 of EPH receptor B6

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 335 of EPH receptor B6

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 EPH receptor B6 between cysteines 124 and 220 (92 and 188 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
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
124
Residue number B
220
Peptide name
EPH receptor B6

Ligandability

Cysteine 124 of EPH receptor B6

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 220 of EPH receptor B6

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 EPH receptor B6 between cysteines 335 and 367 (303 and 335 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
335
Residue number B
367
Peptide name
EPH receptor B6

Ligandability

Cysteine 335 of EPH receptor B6

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 367 of EPH receptor B6

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 EPH receptor B6 between cysteines 114 and 220 (82 and 188 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
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
114
Residue number B
220
Peptide name
EPH receptor B6

Ligandability

Cysteine 114 of EPH receptor B6

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 220 of EPH receptor B6

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 EPH receptor B6 between cysteines 411 and 428 (379 and 396 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
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
411
Residue number B
428
Peptide name
EPH receptor B6

Ligandability

Cysteine 411 of EPH receptor B6

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 428 of EPH receptor B6

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 EPH receptor B6 between cysteines 315 and 332 (283 and 300 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
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
315
Residue number B
332
Peptide name
EPH receptor B6

Ligandability

Cysteine 315 of EPH receptor B6

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 332 of EPH receptor B6

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 EPH receptor B6 between cysteines 349 and 351 (317 and 319 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
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
349
Residue number B
351
Peptide name
EPH receptor B6

Ligandability

Cysteine 349 of EPH receptor B6

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 351 of EPH receptor B6

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 EPH receptor B6 between cysteines 75 and 114 (43 and 82 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
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
75
Residue number B
114
Peptide name
EPH receptor B6

Ligandability

Cysteine 75 of EPH receptor B6

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 114 of EPH receptor B6

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 EPH receptor B6 between cysteines 332 and 349 (300 and 317 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
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
332
Residue number B
349
Peptide name
EPH receptor B6

Ligandability

Cysteine 332 of EPH receptor B6

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 349 of EPH receptor B6

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 EPH receptor B6 between cysteines 302 and 318 (270 and 286 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
302
Residue number B
318
Peptide name
EPH receptor B6

Ligandability

Cysteine 302 of EPH receptor B6

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 318 of EPH receptor B6

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 EPH receptor B6 between cysteines 408 and 425 (376 and 393 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
408
Residue number B
425
Peptide name
EPH receptor B6

Ligandability

Cysteine 408 of EPH receptor B6

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 425 of EPH receptor B6

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 EPH receptor B6 between cysteines 300 and 302 (268 and 270 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
7k7j
Structure name
ephb6 receptor ectodomain
Structure deposition date
2020-09-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
F8WCM8
Residue number A
300
Residue number B
302
Peptide name
EPH receptor B6

Ligandability

Cysteine 300 of EPH receptor B6

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 302 of EPH receptor B6

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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