ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Interleukin-17 receptor C

Intramolecular
Cysteine 265 and cysteine 277
Cysteine 33 and cysteine 110
Cysteine 145 and cysteine 151
Cysteine 343 and cysteine 359
Cysteine 515 and cysteine 529
Cysteine 119 and cysteine 208
Cysteine 154 and cysteine 233
Cysteine 341 and cysteine 391
Cysteine 400 and cysteine 409
Cysteine 439 and cysteine 453
More...
Cysteine 409 and cysteine 439
Cysteine 481 and cysteine 488
Cysteine 409 and cysteine 453
Cysteine 400 and cysteine 439
Cysteine 341 and cysteine 343
Cysteine 400 and cysteine 453
Cysteine 341 and cysteine 359
Cysteine 343 and cysteine 391
Cysteine 359 and cysteine 391
Cysteine 145 and cysteine 154
Cysteine 145 and cysteine 233
A redox-regulated disulphide may form within Interleukin-17 receptor C between cysteines 265 and 277 (194 and 206 respectively in this structure).

Details

Redox score ?
88
PDB code
6hg9
Structure name
crystal structure of the human il-17rc ecd in complex with human il- 17f, crystal form ii
Structure deposition date
2018-08-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NAC3
Residue number A
265
Residue number B
277
Peptide name
Interleukin-17 receptor C

Ligandability

Cysteine 265 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 277 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 Interleukin-17 receptor C between cysteines 33 and 110 (33 and 39 respectively in this structure).

Details

Redox score ?
87
PDB code
6hg4
Structure name
crystal structure of the human il-17rc ecd in complex with human il- 17f
Structure deposition date
2018-08-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NAC3
Residue number A
33
Residue number B
110
Peptide name
Interleukin-17 receptor C

Ligandability

Cysteine 33 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 110 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 Interleukin-17 receptor C between cysteines 145 and 151 (74 and 80 respectively in this structure).

Details

Redox score ?
86
PDB code
6hg9
Structure name
crystal structure of the human il-17rc ecd in complex with human il- 17f, crystal form ii
Structure deposition date
2018-08-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NAC3
Residue number A
145
Residue number B
151
Peptide name
Interleukin-17 receptor C

Ligandability

Cysteine 145 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 151 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 Interleukin-17 receptor C between cysteines 343 and 359 (272 and 288 respectively in this structure).

Details

Redox score ?
85
PDB code
6hg9
Structure name
crystal structure of the human il-17rc ecd in complex with human il- 17f, crystal form ii
Structure deposition date
2018-08-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NAC3
Residue number A
343
Residue number B
359
Peptide name
Interleukin-17 receptor C

Ligandability

Cysteine 343 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 359 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 Interleukin-17 receptor C between cysteines 515 and 529 (444 and 458 respectively in this structure).

Details

Redox score ?
81
PDB code
7uwn
Structure name
structure of the il-17a-il-17ra-il-17rc ternary complex
Structure deposition date
2022-05-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
7
% buried
62
Peptide accession
Q8NAC3
Residue number A
515
Residue number B
529
Peptide name
Interleukin-17 receptor C

Ligandability

Cysteine 515 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 529 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 Interleukin-17 receptor C between cysteines 119 and 208 (48 and 137 respectively in this structure).

Details

Redox score ?
81
PDB code
6hg9
Structure name
crystal structure of the human il-17rc ecd in complex with human il- 17f, crystal form ii
Structure deposition date
2018-08-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NAC3
Residue number A
119
Residue number B
208
Peptide name
Interleukin-17 receptor C

Ligandability

Cysteine 119 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 208 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 Interleukin-17 receptor C between cysteines 154 and 233 (83 and 162 respectively in this structure).

Details

Redox score ?
80
PDB code
6hg9
Structure name
crystal structure of the human il-17rc ecd in complex with human il- 17f, crystal form ii
Structure deposition date
2018-08-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NAC3
Residue number A
154
Residue number B
233
Peptide name
Interleukin-17 receptor C

Ligandability

Cysteine 154 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 233 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 Interleukin-17 receptor C between cysteines 341 and 391 (270 and 320 respectively in this structure).

Details

Redox score ?
80
PDB code
6hg9
Structure name
crystal structure of the human il-17rc ecd in complex with human il- 17f, crystal form ii
Structure deposition date
2018-08-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NAC3
Residue number A
341
Residue number B
391
Peptide name
Interleukin-17 receptor C

Ligandability

Cysteine 341 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 391 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 Interleukin-17 receptor C between cysteines 400 and 409 (329 and 338 respectively in this structure).

Details

Redox score ?
78
PDB code
7uwn
Structure name
structure of the il-17a-il-17ra-il-17rc ternary complex
Structure deposition date
2022-05-03
Thiol separation (Å)
3
Half-sphere exposure sum ?
57
Minimum pKa ?
9
% buried
47
Peptide accession
Q8NAC3
Residue number A
400
Residue number B
409
Peptide name
Interleukin-17 receptor C

Ligandability

Cysteine 400 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 409 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 Interleukin-17 receptor C between cysteines 439 and 453 (368 and 382 respectively in this structure).

Details

Redox score ?
77
PDB code
7uwn
Structure name
structure of the il-17a-il-17ra-il-17rc ternary complex
Structure deposition date
2022-05-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
8
% buried
47
Peptide accession
Q8NAC3
Residue number A
439
Residue number B
453
Peptide name
Interleukin-17 receptor C

Ligandability

Cysteine 439 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 453 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 Interleukin-17 receptor C between cysteines 409 and 439 (338 and 368 respectively in this structure).

Details

Redox score ?
71
PDB code
6hg9
Structure name
crystal structure of the human il-17rc ecd in complex with human il- 17f, crystal form ii
Structure deposition date
2018-08-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NAC3
Residue number A
409
Residue number B
439
Peptide name
Interleukin-17 receptor C

Ligandability

Cysteine 409 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 439 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 Interleukin-17 receptor C between cysteines 481 and 488 (410 and 417 respectively in this structure).

Details

Redox score ?
65
PDB code
7uwn
Structure name
structure of the il-17a-il-17ra-il-17rc ternary complex
Structure deposition date
2022-05-03
Thiol separation (Å)
5
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
20
Peptide accession
Q8NAC3
Residue number A
481
Residue number B
488
Peptide name
Interleukin-17 receptor C

Ligandability

Cysteine 481 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 488 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 Interleukin-17 receptor C between cysteines 409 and 453 (338 and 382 respectively in this structure).

Details

Redox score ?
62
PDB code
6hg9
Structure name
crystal structure of the human il-17rc ecd in complex with human il- 17f, crystal form ii
Structure deposition date
2018-08-23
Thiol separation (Å)
6
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NAC3
Residue number A
409
Residue number B
453
Peptide name
Interleukin-17 receptor C

Ligandability

Cysteine 409 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 453 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 Interleukin-17 receptor C between cysteines 400 and 439 (329 and 368 respectively in this structure).

Details

Redox score ?
60
PDB code
6hg9
Structure name
crystal structure of the human il-17rc ecd in complex with human il- 17f, crystal form ii
Structure deposition date
2018-08-23
Thiol separation (Å)
6
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NAC3
Residue number A
400
Residue number B
439
Peptide name
Interleukin-17 receptor C

Ligandability

Cysteine 400 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 439 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 Interleukin-17 receptor C between cysteines 341 and 343 (270 and 272 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
6hg4
Structure name
crystal structure of the human il-17rc ecd in complex with human il- 17f
Structure deposition date
2018-08-22
Thiol separation (Å)
7
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NAC3
Residue number A
341
Residue number B
343
Peptide name
Interleukin-17 receptor C

Ligandability

Cysteine 341 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 343 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 Interleukin-17 receptor C between cysteines 400 and 453 (329 and 382 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
6hga
Structure name
crystal structure of the human il-17rc d2-d3-d4 domains in complex with an anti-app tag fab
Structure deposition date
2018-08-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NAC3
Residue number A
400
Residue number B
453
Peptide name
Interleukin-17 receptor C

Ligandability

Cysteine 400 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 453 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 Interleukin-17 receptor C between cysteines 341 and 359 (270 and 288 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
6hg4
Structure name
crystal structure of the human il-17rc ecd in complex with human il- 17f
Structure deposition date
2018-08-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NAC3
Residue number A
341
Residue number B
359
Peptide name
Interleukin-17 receptor C

Ligandability

Cysteine 341 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 359 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 Interleukin-17 receptor C between cysteines 343 and 391 (272 and 320 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
6hg4
Structure name
crystal structure of the human il-17rc ecd in complex with human il- 17f
Structure deposition date
2018-08-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NAC3
Residue number A
343
Residue number B
391
Peptide name
Interleukin-17 receptor C

Ligandability

Cysteine 343 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 391 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 Interleukin-17 receptor C between cysteines 359 and 391 (288 and 320 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
6hg9
Structure name
crystal structure of the human il-17rc ecd in complex with human il- 17f, crystal form ii
Structure deposition date
2018-08-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NAC3
Residue number A
359
Residue number B
391
Peptide name
Interleukin-17 receptor C

Ligandability

Cysteine 359 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 391 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 Interleukin-17 receptor C between cysteines 145 and 154 (74 and 83 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
6hg9
Structure name
crystal structure of the human il-17rc ecd in complex with human il- 17f, crystal form ii
Structure deposition date
2018-08-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NAC3
Residue number A
145
Residue number B
154
Peptide name
Interleukin-17 receptor C

Ligandability

Cysteine 145 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 154 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 Interleukin-17 receptor C between cysteines 145 and 233 (74 and 162 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
6hg4
Structure name
crystal structure of the human il-17rc ecd in complex with human il- 17f
Structure deposition date
2018-08-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NAC3
Residue number A
145
Residue number B
233
Peptide name
Interleukin-17 receptor C

Ligandability

Cysteine 145 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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 233 of Interleukin-17 receptor C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in 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.

If this tool was useful for finding a disulphide, please cite: