ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Insulin receptor-related protein

Intramolecular
Cysteine 304 and cysteine 317
Cysteine 30 and cysteine 48
Cysteine 262 and cysteine 274
Cysteine 216 and cysteine 228
Cysteine 320 and cysteine 324
Cysteine 229 and cysteine 237
Cysteine 191 and cysteine 210
Cysteine 280 and cysteine 300
Cysteine 148 and cysteine 176
Cysteine 657 and cysteine 864
More...
Cysteine 233 and cysteine 246
Cysteine 249 and cysteine 258
Cysteine 328 and cysteine 347
Cysteine 214 and cysteine 222
Cysteine 180 and cysteine 204
Cysteine 449 and cysteine 482
Cysteine 790 and cysteine 799
Cysteine 214 and cysteine 216
Cysteine 246 and cysteine 258
Cysteine 214 and cysteine 228
Cysteine 191 and cysteine 204
Cysteine 233 and cysteine 237
Cysteine 222 and cysteine 228
Cysteine 229 and cysteine 233
Cysteine 246 and cysteine 249
Cysteine 233 and cysteine 258
Cysteine 216 and cysteine 222
Cysteine 237 and cysteine 246
Cysteine 180 and cysteine 191
Cysteine 222 and cysteine 229
Cysteine 229 and cysteine 246
Cysteine 204 and cysteine 210
Cysteine 180 and cysteine 210
Cysteine 228 and cysteine 229
Cysteine 304 and cysteine 320
Cysteine 216 and cysteine 229
Cysteine 233 and cysteine 249
Cysteine 216 and cysteine 237
Cysteine 300 and cysteine 317
Cysteine 304 and cysteine 324
A redox-regulated disulphide may form within Insulin receptor-related protein between cysteines 304 and 317 (278 and 291 respectively in this structure).

Details

Redox score ?
89
PDB code
7tyk
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in apo- state captured at ph 7
Structure deposition date
2022-02-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
304
Residue number B
317
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 304 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 317 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 30 and 48 (4 and 22 respectively in this structure).

Details

Redox score ?
87
PDB code
7tyk
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in apo- state captured at ph 7
Structure deposition date
2022-02-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
30
Residue number B
48
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 30 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 48 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 262 and 274 (236 and 248 respectively in this structure).

Details

Redox score ?
87
PDB code
7tym
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in active-state captured at ph 9
Structure deposition date
2022-02-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
262
Residue number B
274
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 262 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 274 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 216 and 228 (190 and 202 respectively in this structure).

Details

Redox score ?
86
PDB code
7tyk
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in apo- state captured at ph 7
Structure deposition date
2022-02-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
216
Residue number B
228
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 216 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 228 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 320 and 324 (294 and 298 respectively in this structure).

Details

Redox score ?
85
PDB code
7tyk
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in apo- state captured at ph 7
Structure deposition date
2022-02-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
8
% buried
0
Peptide accession
P14616
Residue number A
320
Residue number B
324
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 320 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 324 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 229 and 237 (203 and 211 respectively in this structure).

Details

Redox score ?
85
PDB code
7tyk
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in apo- state captured at ph 7
Structure deposition date
2022-02-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
229
Residue number B
237
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 229 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 237 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 191 and 210 (165 and 184 respectively in this structure).

Details

Redox score ?
85
PDB code
7tyj
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in apo- state captured at ph 7
Structure deposition date
2022-02-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
191
Residue number B
210
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 191 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 210 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 280 and 300 (254 and 274 respectively in this structure).

Details

Redox score ?
85
PDB code
7tym
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in active-state captured at ph 9
Structure deposition date
2022-02-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
280
Residue number B
300
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 280 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 148 and 176 (122 and 150 respectively in this structure).

Details

Redox score ?
84
PDB code
7tym
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in active-state captured at ph 9
Structure deposition date
2022-02-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
148
Residue number B
176
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 148 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 176 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 657 and 864 (631 and 838 respectively in this structure).

Details

Redox score ?
83
PDB code
7tym
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in active-state captured at ph 9
Structure deposition date
2022-02-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
657
Residue number B
864
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 657 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 864 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 233 and 246 (207 and 220 respectively in this structure).

Details

Redox score ?
83
PDB code
7tyk
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in apo- state captured at ph 7
Structure deposition date
2022-02-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
233
Residue number B
246
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 233 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 246 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 249 and 258 (223 and 232 respectively in this structure).

Details

Redox score ?
82
PDB code
7tyk
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in apo- state captured at ph 7
Structure deposition date
2022-02-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
249
Residue number B
258
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 249 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 258 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 328 and 347 (302 and 321 respectively in this structure).

Details

Redox score ?
82
PDB code
7tym
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in active-state captured at ph 9
Structure deposition date
2022-02-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
328
Residue number B
347
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 328 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 347 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 214 and 222 (188 and 196 respectively in this structure).

Details

Redox score ?
81
PDB code
7tym
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in active-state captured at ph 9
Structure deposition date
2022-02-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
214
Residue number B
222
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 214 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 222 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 180 and 204 (154 and 178 respectively in this structure).

Details

Redox score ?
81
PDB code
7tyk
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in apo- state captured at ph 7
Structure deposition date
2022-02-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
180
Residue number B
204
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 180 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 204 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 449 and 482 (423 and 456 respectively in this structure).

Details

Redox score ?
81
PDB code
7tyk
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in apo- state captured at ph 7
Structure deposition date
2022-02-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
449
Residue number B
482
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 449 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 482 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 790 and 799 (764 and 773 respectively in this structure).

Details

Redox score ?
79
PDB code
7tyj
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in apo- state captured at ph 7
Structure deposition date
2022-02-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
790
Residue number B
799
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 790 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 799 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 214 and 216 (188 and 190 respectively in this structure).

Details

Redox score ?
76
PDB code
7tym
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in active-state captured at ph 9
Structure deposition date
2022-02-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
214
Residue number B
216
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 214 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 216 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 246 and 258 (220 and 232 respectively in this structure).

Details

Redox score ?
76
PDB code
7tyk
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in apo- state captured at ph 7
Structure deposition date
2022-02-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
246
Residue number B
258
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 246 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 258 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 214 and 228 (188 and 202 respectively in this structure).

Details

Redox score ?
75
PDB code
7tyk
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in apo- state captured at ph 7
Structure deposition date
2022-02-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
214
Residue number B
228
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 214 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 228 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 191 and 204 (165 and 178 respectively in this structure).

Details

Redox score ?
68
PDB code
7tym
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in active-state captured at ph 9
Structure deposition date
2022-02-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
191
Residue number B
204
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 191 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 204 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 233 and 237 (207 and 211 respectively in this structure).

Details

Redox score ?
67
PDB code
7tym
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in active-state captured at ph 9
Structure deposition date
2022-02-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
233
Residue number B
237
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 233 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 237 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 222 and 228 (196 and 202 respectively in this structure).

Details

Redox score ?
66
PDB code
7tym
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in active-state captured at ph 9
Structure deposition date
2022-02-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
222
Residue number B
228
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 222 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 228 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 229 and 233 (203 and 207 respectively in this structure).

Details

Redox score ?
65
PDB code
7tyj
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in apo- state captured at ph 7
Structure deposition date
2022-02-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
229
Residue number B
233
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 229 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 246 and 249 (220 and 223 respectively in this structure).

Details

Redox score ?
62
PDB code
7tyj
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in apo- state captured at ph 7
Structure deposition date
2022-02-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
246
Residue number B
249
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 246 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 249 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 233 and 258 (207 and 232 respectively in this structure).

Details

Redox score ?
62
PDB code
7tyk
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in apo- state captured at ph 7
Structure deposition date
2022-02-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
233
Residue number B
258
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 233 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 258 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 216 and 222 (190 and 196 respectively in this structure).

Details

Redox score ?
60
PDB code
7tyj
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in apo- state captured at ph 7
Structure deposition date
2022-02-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
216
Residue number B
222
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 216 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 222 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 237 and 246 (211 and 220 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
7tyk
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in apo- state captured at ph 7
Structure deposition date
2022-02-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
237
Residue number B
246
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 237 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 246 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 180 and 191 (154 and 165 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
7tyk
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in apo- state captured at ph 7
Structure deposition date
2022-02-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
180
Residue number B
191
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 180 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 191 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 222 and 229 (196 and 203 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
7tyk
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in apo- state captured at ph 7
Structure deposition date
2022-02-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
222
Residue number B
229
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 222 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 229 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 229 and 246 (203 and 220 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
7tyk
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in apo- state captured at ph 7
Structure deposition date
2022-02-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
229
Residue number B
246
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 229 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 246 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 204 and 210 (178 and 184 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
7tyj
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in apo- state captured at ph 7
Structure deposition date
2022-02-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
204
Residue number B
210
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 204 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 210 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 180 and 210 (154 and 184 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
7tyj
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in apo- state captured at ph 7
Structure deposition date
2022-02-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
180
Residue number B
210
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 180 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 210 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 228 and 229 (202 and 203 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
7tym
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in active-state captured at ph 9
Structure deposition date
2022-02-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
228
Residue number B
229
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 228 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 229 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 304 and 320 (278 and 294 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
7tyj
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in apo- state captured at ph 7
Structure deposition date
2022-02-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
47
Minimum pKa ?
10
% buried
nan
Peptide accession
P14616
Residue number A
304
Residue number B
320
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 304 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 320 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 216 and 229 (190 and 203 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
7tyj
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in apo- state captured at ph 7
Structure deposition date
2022-02-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
216
Residue number B
229
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 216 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 229 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 233 and 249 (207 and 223 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
7tyj
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in apo- state captured at ph 7
Structure deposition date
2022-02-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
233
Residue number B
249
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 233 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 249 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 216 and 237 (190 and 211 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
7tym
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in active-state captured at ph 9
Structure deposition date
2022-02-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
216
Residue number B
237
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 216 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 237 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 300 and 317 (274 and 291 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
7tyj
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in apo- state captured at ph 7
Structure deposition date
2022-02-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14616
Residue number A
300
Residue number B
317
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 300 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 317 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Insulin receptor-related protein between cysteines 304 and 324 (278 and 298 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
7tyj
Structure name
cryo-em structure of insulin receptor-related receptor (irr) in apo- state captured at ph 7
Structure deposition date
2022-02-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
53
Minimum pKa ?
8
% buried
nan
Peptide accession
P14616
Residue number A
304
Residue number B
324
Peptide name
Insulin receptor-related protein

Ligandability

Cysteine 304 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 324 of Insulin receptor-related protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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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