Insulin-like growth factor 1 receptor
Intermolecular
Cysteine 701 and cysteine 701
Cysteine 544 and cysteine 551 of Insulin receptor
Cysteine 701 and cysteine 703
Intramolecular
Cysteine 699 and cysteine 702
Cysteine 307 and cysteine 321
Cysteine 192 and cysteine 211
Cysteine 264 and cysteine 276
Cysteine 33 and cysteine 52
Cysteine 231 and cysteine 239
Cysteine 219 and cysteine 230
More...Cysteine 235 and cysteine 248
Cysteine 215 and cysteine 224
Cysteine 150 and cysteine 178
Cysteine 182 and cysteine 205
Cysteine 663 and cysteine 879
Cysteine 282 and cysteine 303
Cysteine 332 and cysteine 353
Cysteine 251 and cysteine 260
Cysteine 807 and cysteine 816
Cysteine 248 and cysteine 260
Cysteine 235 and cysteine 239
Cysteine 192 and cysteine 205
Cysteine 182 and cysteine 192
Cysteine 324 and cysteine 328
Cysteine 239 and cysteine 248
Cysteine 456 and cysteine 489
Cysteine 215 and cysteine 219
Cysteine 205 and cysteine 211
Cysteine 231 and cysteine 235
Cysteine 219 and cysteine 224
Cysteine 235 and cysteine 260
Cysteine 248 and cysteine 251
Cysteine 231 and cysteine 248
Cysteine 215 and cysteine 231
Cysteine 230 and cysteine 231
Cysteine 219 and cysteine 231
Cysteine 307 and cysteine 328
Cysteine 182 and cysteine 211
Cysteine 699 and cysteine 700
Cysteine 215 and cysteine 230
6pyh A 671 D 671
A redox-regulated disulphide may form between two units of Insulin-like growth factor 1 receptor at cysteines 701 and 701 (671 and 671 respectively in this structure).
Details
Redox score ?
94
PDB code
6pyh
Structure name
cryo-em structure of full-length igf1r-igf1 complex
Structure deposition date
2019-07-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin-like growth factor 1 receptor
Peptide B name
Insulin-like growth factor 1 receptor
Peptide A accession
Q60751
Peptide B accession
Q60751
Peptide A residue number
701
Peptide B residue number
701
Ligandability
7s0q A 514 B 524
A redox-regulated disulphide may form between cysteine 544 of Insulin-like growth factor 1 receptor and cysteine 551 of Insulin receptor (514 and 524 respectively in this structure).
Details
Redox score ?
83
PDB code
7s0q
Structure name
head region of a complex of igf-i with the ectodomain of a hybrid insulin receptor / type 1 insulin-like growth factor receptor
Structure deposition date
2021-08-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin-like growth factor 1 receptor
Peptide B name
Insulin receptor
Peptide A accession
P08069
Peptide B accession
P06213
Peptide A residue number
544
Peptide B residue number
551
Ligandability
Cysteine 544 of Insulin-like growth factor 1 receptor
Cysteine 551 of Insulin receptor
6pyh A 671 D 673
A redox-regulated disulphide may form between two units of Insulin-like growth factor 1 receptor at cysteines 701 and 703 (671 and 673 respectively in this structure).
Details
Redox score ?
61
PDB code
6pyh
Structure name
cryo-em structure of full-length igf1r-igf1 complex
Structure deposition date
2019-07-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
nan
Peptide A name
Insulin-like growth factor 1 receptor
Peptide B name
Insulin-like growth factor 1 receptor
Peptide A accession
Q60751
Peptide B accession
Q60751
Peptide A residue number
701
Peptide B residue number
703
Ligandability
Cysteine 701 of Insulin-like growth factor 1 receptor
Cysteine 703 of Insulin-like growth factor 1 receptor
6jk8 A 700 A 703
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 699 and 702 (700 and 703 respectively in this structure).
Details
Redox score ?
90
PDB code
6jk8
Structure name
cryo-em structure of the full-length human igf-1r in complex with insulin
Structure deposition date
2019-02-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
21
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
699
Residue number B
702
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 699 of Insulin-like growth factor 1 receptor
Cysteine 702 of Insulin-like growth factor 1 receptor
5u8q A 277 A 291
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 307 and 321 (277 and 291 respectively in this structure).
Details
Redox score ?
88
PDB code
5u8q
Structure name
structure of the ectodomain of the human type 1 insulin-like growth factor receptor in complex with igf-i
Structure deposition date
2016-12-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
307
Residue number B
321
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 307 of Insulin-like growth factor 1 receptor
Cysteine 321 of Insulin-like growth factor 1 receptor
5u8r A 162 A 181
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 192 and 211 (162 and 181 respectively in this structure).
Details
Redox score ?
88
PDB code
5u8r
Structure name
structure of the ectodomain of the human type 1 insulin-like growth factor receptor
Structure deposition date
2016-12-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
192
Residue number B
211
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 192 of Insulin-like growth factor 1 receptor
Cysteine 211 of Insulin-like growth factor 1 receptor
1igr A 234 A 246
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 264 and 276 (234 and 246 respectively in this structure).
Details
Redox score ?
88
PDB code
1igr
Structure name
type 1 insulin-like growth factor receptor (domains 1-3)
Structure deposition date
1998-09-28
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
264
Residue number B
276
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 264 of Insulin-like growth factor 1 receptor
Cysteine 276 of Insulin-like growth factor 1 receptor
6pyh A 3 A 22
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 33 and 52 (3 and 22 respectively in this structure).
Details
Redox score ?
87
PDB code
6pyh
Structure name
cryo-em structure of full-length igf1r-igf1 complex
Structure deposition date
2019-07-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q60751
Residue number A
33
Residue number B
52
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 33 of Insulin-like growth factor 1 receptor
Cysteine 52 of Insulin-like growth factor 1 receptor
5u8r A 201 A 209
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 231 and 239 (201 and 209 respectively in this structure).
Details
Redox score ?
86
PDB code
5u8r
Structure name
structure of the ectodomain of the human type 1 insulin-like growth factor receptor
Structure deposition date
2016-12-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
231
Residue number B
239
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 231 of Insulin-like growth factor 1 receptor
Cysteine 239 of Insulin-like growth factor 1 receptor
5u8r A 189 A 200
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 219 and 230 (189 and 200 respectively in this structure).
Details
Redox score ?
85
PDB code
5u8r
Structure name
structure of the ectodomain of the human type 1 insulin-like growth factor receptor
Structure deposition date
2016-12-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
219
Residue number B
230
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 219 of Insulin-like growth factor 1 receptor
Cysteine 230 of Insulin-like growth factor 1 receptor
5u8q A 205 A 218
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 235 and 248 (205 and 218 respectively in this structure).
Details
Redox score ?
85
PDB code
5u8q
Structure name
structure of the ectodomain of the human type 1 insulin-like growth factor receptor in complex with igf-i
Structure deposition date
2016-12-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
235
Residue number B
248
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 235 of Insulin-like growth factor 1 receptor
Cysteine 248 of Insulin-like growth factor 1 receptor
5u8r A 185 A 194
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 215 and 224 (185 and 194 respectively in this structure).
Details
Redox score ?
84
PDB code
5u8r
Structure name
structure of the ectodomain of the human type 1 insulin-like growth factor receptor
Structure deposition date
2016-12-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
215
Residue number B
224
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 215 of Insulin-like growth factor 1 receptor
Cysteine 224 of Insulin-like growth factor 1 receptor
5u8q A 120 A 148
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 150 and 178 (120 and 148 respectively in this structure).
Details
Redox score ?
84
PDB code
5u8q
Structure name
structure of the ectodomain of the human type 1 insulin-like growth factor receptor in complex with igf-i
Structure deposition date
2016-12-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
150
Residue number B
178
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 150 of Insulin-like growth factor 1 receptor
Cysteine 178 of Insulin-like growth factor 1 receptor
5u8r A 152 A 175
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 182 and 205 (152 and 175 respectively in this structure).
Details
Redox score ?
84
PDB code
5u8r
Structure name
structure of the ectodomain of the human type 1 insulin-like growth factor receptor
Structure deposition date
2016-12-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
182
Residue number B
205
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 182 of Insulin-like growth factor 1 receptor
Cysteine 205 of Insulin-like growth factor 1 receptor
5u8q A 633 A 849
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 663 and 879 (633 and 849 respectively in this structure).
Details
Redox score ?
83
PDB code
5u8q
Structure name
structure of the ectodomain of the human type 1 insulin-like growth factor receptor in complex with igf-i
Structure deposition date
2016-12-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
663
Residue number B
879
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 663 of Insulin-like growth factor 1 receptor
Cysteine 879 of Insulin-like growth factor 1 receptor
5u8r A 252 A 273
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 282 and 303 (252 and 273 respectively in this structure).
Details
Redox score ?
83
PDB code
5u8r
Structure name
structure of the ectodomain of the human type 1 insulin-like growth factor receptor
Structure deposition date
2016-12-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
282
Residue number B
303
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 282 of Insulin-like growth factor 1 receptor
Cysteine 303 of Insulin-like growth factor 1 receptor
5u8r A 302 A 323
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 332 and 353 (302 and 323 respectively in this structure).
Details
Redox score ?
82
PDB code
5u8r
Structure name
structure of the ectodomain of the human type 1 insulin-like growth factor receptor
Structure deposition date
2016-12-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
332
Residue number B
353
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 332 of Insulin-like growth factor 1 receptor
Cysteine 353 of Insulin-like growth factor 1 receptor
5u8q A 221 A 230
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 251 and 260 (221 and 230 respectively in this structure).
Details
Redox score ?
81
PDB code
5u8q
Structure name
structure of the ectodomain of the human type 1 insulin-like growth factor receptor in complex with igf-i
Structure deposition date
2016-12-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
251
Residue number B
260
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 251 of Insulin-like growth factor 1 receptor
Cysteine 260 of Insulin-like growth factor 1 receptor
8eyr B 781 B 790
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 807 and 816 (781 and 790 respectively in this structure).
Details
Redox score ?
81
PDB code
8eyr
Structure name
cryo-em structure of two igf1 bound full-length mouse igf1r mutant (four glycine residues inserted in the alpha-ct; igf1r-p674g4): symmetric conformation
Structure deposition date
2022-10-28
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q60751
Residue number A
807
Residue number B
816
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 807 of Insulin-like growth factor 1 receptor
Cysteine 816 of Insulin-like growth factor 1 receptor
1igr A 218 A 230
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 248 and 260 (218 and 230 respectively in this structure).
Details
Redox score ?
79
PDB code
1igr
Structure name
type 1 insulin-like growth factor receptor (domains 1-3)
Structure deposition date
1998-09-28
Thiol separation (Å)
3
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
248
Residue number B
260
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 248 of Insulin-like growth factor 1 receptor
Cysteine 260 of Insulin-like growth factor 1 receptor
5u8q A 205 A 209
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 235 and 239 (205 and 209 respectively in this structure).
Details
Redox score ?
78
PDB code
5u8q
Structure name
structure of the ectodomain of the human type 1 insulin-like growth factor receptor in complex with igf-i
Structure deposition date
2016-12-14
Thiol separation (Å)
3
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
235
Residue number B
239
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 235 of Insulin-like growth factor 1 receptor
Cysteine 239 of Insulin-like growth factor 1 receptor
5u8q A 162 A 175
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 192 and 205 (162 and 175 respectively in this structure).
Details
Redox score ?
78
PDB code
5u8q
Structure name
structure of the ectodomain of the human type 1 insulin-like growth factor receptor in complex with igf-i
Structure deposition date
2016-12-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
192
Residue number B
205
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 192 of Insulin-like growth factor 1 receptor
Cysteine 205 of Insulin-like growth factor 1 receptor
5u8r A 152 A 162
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 182 and 192 (152 and 162 respectively in this structure).
Details
Redox score ?
74
PDB code
5u8r
Structure name
structure of the ectodomain of the human type 1 insulin-like growth factor receptor
Structure deposition date
2016-12-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
182
Residue number B
192
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 182 of Insulin-like growth factor 1 receptor
Cysteine 192 of Insulin-like growth factor 1 receptor
6jk8 B 324 B 328
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 324 and 328.
Details
Redox score ?
74
PDB code
6jk8
Structure name
cryo-em structure of the full-length human igf-1r in complex with insulin
Structure deposition date
2019-02-27
Thiol separation (Å)
6
Half-sphere exposure sum ?
45
Minimum pKa ?
8
% buried
2
Peptide accession
P08069
Residue number A
324
Residue number B
328
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 324 of Insulin-like growth factor 1 receptor
Cysteine 328 of Insulin-like growth factor 1 receptor
5u8q A 209 A 218
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 239 and 248 (209 and 218 respectively in this structure).
Details
Redox score ?
73
PDB code
5u8q
Structure name
structure of the ectodomain of the human type 1 insulin-like growth factor receptor in complex with igf-i
Structure deposition date
2016-12-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
239
Residue number B
248
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 239 of Insulin-like growth factor 1 receptor
Cysteine 248 of Insulin-like growth factor 1 receptor
8eyr B 426 B 459
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 456 and 489 (426 and 459 respectively in this structure).
Details
Redox score ?
73
PDB code
8eyr
Structure name
cryo-em structure of two igf1 bound full-length mouse igf1r mutant (four glycine residues inserted in the alpha-ct; igf1r-p674g4): symmetric conformation
Structure deposition date
2022-10-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
8
% buried
42
Peptide accession
Q60751
Residue number A
456
Residue number B
489
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 456 of Insulin-like growth factor 1 receptor
Cysteine 489 of Insulin-like growth factor 1 receptor
5u8q A 185 A 189
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 215 and 219 (185 and 189 respectively in this structure).
Details
Redox score ?
72
PDB code
5u8q
Structure name
structure of the ectodomain of the human type 1 insulin-like growth factor receptor in complex with igf-i
Structure deposition date
2016-12-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
215
Residue number B
219
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 215 of Insulin-like growth factor 1 receptor
Cysteine 219 of Insulin-like growth factor 1 receptor
5u8q A 175 A 181
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 205 and 211 (175 and 181 respectively in this structure).
Details
Redox score ?
72
PDB code
5u8q
Structure name
structure of the ectodomain of the human type 1 insulin-like growth factor receptor in complex with igf-i
Structure deposition date
2016-12-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
205
Residue number B
211
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 205 of Insulin-like growth factor 1 receptor
Cysteine 211 of Insulin-like growth factor 1 receptor
5u8r A 201 A 205
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 231 and 235 (201 and 205 respectively in this structure).
Details
Redox score ?
70
PDB code
5u8r
Structure name
structure of the ectodomain of the human type 1 insulin-like growth factor receptor
Structure deposition date
2016-12-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
231
Residue number B
235
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 231 of Insulin-like growth factor 1 receptor
Cysteine 235 of Insulin-like growth factor 1 receptor
5u8q A 189 A 194
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 219 and 224 (189 and 194 respectively in this structure).
Details
Redox score ?
67
PDB code
5u8q
Structure name
structure of the ectodomain of the human type 1 insulin-like growth factor receptor in complex with igf-i
Structure deposition date
2016-12-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
219
Residue number B
224
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 219 of Insulin-like growth factor 1 receptor
Cysteine 224 of Insulin-like growth factor 1 receptor
5u8q A 205 A 230
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 235 and 260 (205 and 230 respectively in this structure).
Details
Redox score ?
66
PDB code
5u8q
Structure name
structure of the ectodomain of the human type 1 insulin-like growth factor receptor in complex with igf-i
Structure deposition date
2016-12-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
235
Residue number B
260
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 235 of Insulin-like growth factor 1 receptor
Cysteine 260 of Insulin-like growth factor 1 receptor
1igr A 218 A 221
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 248 and 251 (218 and 221 respectively in this structure).
Details
Redox score ?
63
PDB code
1igr
Structure name
type 1 insulin-like growth factor receptor (domains 1-3)
Structure deposition date
1998-09-28
Thiol separation (Å)
5
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
248
Residue number B
251
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 248 of Insulin-like growth factor 1 receptor
Cysteine 251 of Insulin-like growth factor 1 receptor
5u8r A 201 A 218
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 231 and 248 (201 and 218 respectively in this structure).
Details
Redox score ?
63
PDB code
5u8r
Structure name
structure of the ectodomain of the human type 1 insulin-like growth factor receptor
Structure deposition date
2016-12-14
Thiol separation (Å)
6
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
231
Residue number B
248
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 231 of Insulin-like growth factor 1 receptor
Cysteine 248 of Insulin-like growth factor 1 receptor
5u8q A 185 A 201
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 215 and 231 (185 and 201 respectively in this structure).
Details
Redox score ?
61
PDB code
5u8q
Structure name
structure of the ectodomain of the human type 1 insulin-like growth factor receptor in complex with igf-i
Structure deposition date
2016-12-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
215
Residue number B
231
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 215 of Insulin-like growth factor 1 receptor
Cysteine 231 of Insulin-like growth factor 1 receptor
8eyr B 200 B 201
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 230 and 231 (200 and 201 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
8eyr
Structure name
cryo-em structure of two igf1 bound full-length mouse igf1r mutant (four glycine residues inserted in the alpha-ct; igf1r-p674g4): symmetric conformation
Structure deposition date
2022-10-28
Thiol separation (Å)
6
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q60751
Residue number A
230
Residue number B
231
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 230 of Insulin-like growth factor 1 receptor
Cysteine 231 of Insulin-like growth factor 1 receptor
5u8q A 189 A 201
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 219 and 231 (189 and 201 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
5u8q
Structure name
structure of the ectodomain of the human type 1 insulin-like growth factor receptor in complex with igf-i
Structure deposition date
2016-12-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
219
Residue number B
231
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 219 of Insulin-like growth factor 1 receptor
Cysteine 231 of Insulin-like growth factor 1 receptor
6pyh A 277 A 298
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 307 and 328 (277 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 ?
56
PDB code
6pyh
Structure name
cryo-em structure of full-length igf1r-igf1 complex
Structure deposition date
2019-07-29
Thiol separation (Å)
8
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
nan
Peptide accession
Q60751
Residue number A
307
Residue number B
328
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 307 of Insulin-like growth factor 1 receptor
Cysteine 328 of Insulin-like growth factor 1 receptor
6pyh A 152 A 181
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 182 and 211 (152 and 181 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
6pyh
Structure name
cryo-em structure of full-length igf1r-igf1 complex
Structure deposition date
2019-07-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q60751
Residue number A
182
Residue number B
211
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 182 of Insulin-like growth factor 1 receptor
Cysteine 211 of Insulin-like growth factor 1 receptor
6jk8 A 700 A 701
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 699 and 700 (700 and 701 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
6jk8
Structure name
cryo-em structure of the full-length human igf-1r in complex with insulin
Structure deposition date
2019-02-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
16
Minimum pKa ?
9
% buried
nan
Peptide accession
P08069
Residue number A
699
Residue number B
700
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 699 of Insulin-like growth factor 1 receptor
Cysteine 700 of Insulin-like growth factor 1 receptor
5u8q A 185 A 200
A redox-regulated disulphide may form within Insulin-like growth factor 1 receptor between cysteines 215 and 230 (185 and 200 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
5u8q
Structure name
structure of the ectodomain of the human type 1 insulin-like growth factor receptor in complex with igf-i
Structure deposition date
2016-12-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08069
Residue number A
215
Residue number B
230
Peptide name
Insulin-like growth factor 1 receptor
Ligandability
Cysteine 215 of Insulin-like growth factor 1 receptor
Cysteine 230 of Insulin-like growth factor 1 receptor
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