Receptor tyrosine-protein kinase erbB-2
Intramolecular
Cysteine 630 and cysteine 642
Cysteine 826 and cysteine 53
Cysteine 626 and cysteine 634
Cysteine 162 and cysteine 965
Cysteine 299 and cysteine 311
Cysteine 334 and cysteine 338
Cysteine 268 and cysteine 295
Cysteine 600 and cysteine 623
Cysteine 199 and cysteine 212
Cysteine 315 and cysteine 331
More...Cysteine 531 and cysteine 540
Cysteine 342 and cysteine 367
Cysteine 544 and cysteine 560
Cysteine 224 and cysteine 235
Cysteine 240 and cysteine 252
Cysteine 236 and cysteine 244
Cysteine 511 and cysteine 520
Cysteine 26 and cysteine 53
Cysteine 162 and cysteine 192
Cysteine 475 and cysteine 504
Cysteine 195 and cysteine 199
Cysteine 587 and cysteine 596
Cysteine 563 and cysteine 576
Cysteine 195 and cysteine 204
Cysteine 511 and cysteine 515
Cysteine 515 and cysteine 528
Cysteine 252 and cysteine 264
Cysteine 220 and cysteine 227
Cysteine 567 and cysteine 576
Cysteine 224 and cysteine 227
Cysteine 528 and cysteine 540
Cysteine 584 and cysteine 596
Cysteine 255 and cysteine 264
Cysteine 220 and cysteine 224
Cysteine 240 and cysteine 244
Cysteine 240 and cysteine 264
Cysteine 584 and cysteine 587
Cysteine 567 and cysteine 584
Cysteine 199 and cysteine 204
Cysteine 515 and cysteine 520
3n85 A 608 A 620
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 630 and 642 (608 and 620 respectively in this structure).
Details
Redox score ?
91
PDB code
3n85
Structure name
crystallographic trimer of her2 extracellular regions in complex with tryptophan-rich antibody fragment
Structure deposition date
2010-05-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
630
Residue number B
642
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 630 of Receptor tyrosine-protein kinase erbB-2
Cysteine 642 of Receptor tyrosine-protein kinase erbB-2
4hrm C 4 C 31
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 826 and 53 (4 and 31 respectively in this structure).
Details
Redox score ?
90
PDB code
4hrm
Structure name
structural basis for eliciting a cytotoxic effect in her2- overexpressing cancer cells via binding to the extracellular domain of her2
Structure deposition date
2012-10-28
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
826
Residue number B
53
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 826 of Receptor tyrosine-protein kinase erbB-2
Cysteine 53 of Receptor tyrosine-protein kinase erbB-2
3n85 A 604 A 612
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 626 and 634 (604 and 612 respectively in this structure).
Details
Redox score ?
88
PDB code
3n85
Structure name
crystallographic trimer of her2 extracellular regions in complex with tryptophan-rich antibody fragment
Structure deposition date
2010-05-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
626
Residue number B
634
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 626 of Receptor tyrosine-protein kinase erbB-2
Cysteine 634 of Receptor tyrosine-protein kinase erbB-2
4hrm A 140 A 170
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 162 and 965 (140 and 170 respectively in this structure).
Details
Redox score ?
87
PDB code
4hrm
Structure name
structural basis for eliciting a cytotoxic effect in her2- overexpressing cancer cells via binding to the extracellular domain of her2
Structure deposition date
2012-10-28
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
162
Residue number B
965
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 162 of Receptor tyrosine-protein kinase erbB-2
Cysteine 965 of Receptor tyrosine-protein kinase erbB-2
3wlw A 277 A 289
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 299 and 311 (277 and 289 respectively in this structure).
Details
Redox score ?
87
PDB code
3wlw
Structure name
molecular architecture of the erbb2 extracellular domain homodimer
Structure deposition date
2013-11-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
299
Residue number B
311
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 299 of Receptor tyrosine-protein kinase erbB-2
Cysteine 311 of Receptor tyrosine-protein kinase erbB-2
5o4g C 312 C 316
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 334 and 338 (312 and 316 respectively in this structure).
Details
Redox score ?
87
PDB code
5o4g
Structure name
her2 in complex with fab mf3958
Structure deposition date
2017-05-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
32
Minimum pKa ?
9
% buried
0
Peptide accession
P04626
Residue number A
334
Residue number B
338
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 334 of Receptor tyrosine-protein kinase erbB-2
Cysteine 338 of Receptor tyrosine-protein kinase erbB-2
5my6 A 268 A 295
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 268 and 295.
Details
Redox score ?
86
PDB code
5my6
Structure name
crystal structure of a her2-nb complex
Structure deposition date
2017-01-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
268
Residue number B
295
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 268 of Receptor tyrosine-protein kinase erbB-2
Cysteine 295 of Receptor tyrosine-protein kinase erbB-2
6bgt C 578 C 601
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 600 and 623 (578 and 601 respectively in this structure).
Details
Redox score ?
86
PDB code
6bgt
Structure name
structure of trastuzumab fab mutant in complex with her2 extracellular domain
Structure deposition date
2017-10-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
600
Residue number B
623
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 600 of Receptor tyrosine-protein kinase erbB-2
Cysteine 623 of Receptor tyrosine-protein kinase erbB-2
5k33 C 177 C 190
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 199 and 212 (177 and 190 respectively in this structure).
Details
Redox score ?
86
PDB code
5k33
Structure name
crystal structure of extracellular domain of her2 in complex with fcab stab19
Structure deposition date
2016-05-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
199
Residue number B
212
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 199 of Receptor tyrosine-protein kinase erbB-2
Cysteine 212 of Receptor tyrosine-protein kinase erbB-2
1s78 A 293 A 309
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 315 and 331 (293 and 309 respectively in this structure).
Details
Redox score ?
86
PDB code
1s78
Structure name
insights into erbb signaling from the structure of the erbb2- pertuzumab complex
Structure deposition date
2004-01-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
315
Residue number B
331
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 315 of Receptor tyrosine-protein kinase erbB-2
Cysteine 331 of Receptor tyrosine-protein kinase erbB-2
5k33 C 509 C 518
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 531 and 540 (509 and 518 respectively in this structure).
Details
Redox score ?
85
PDB code
5k33
Structure name
crystal structure of extracellular domain of her2 in complex with fcab stab19
Structure deposition date
2016-05-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
531
Residue number B
540
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 531 of Receptor tyrosine-protein kinase erbB-2
Cysteine 540 of Receptor tyrosine-protein kinase erbB-2
3wsq A 320 A 345
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 342 and 367 (320 and 345 respectively in this structure).
Details
Redox score ?
85
PDB code
3wsq
Structure name
structure of her2 with an fab
Structure deposition date
2014-03-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
342
Residue number B
367
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 342 of Receptor tyrosine-protein kinase erbB-2
Cysteine 367 of Receptor tyrosine-protein kinase erbB-2
5my6 A 544 A 560
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 544 and 560.
Details
Redox score ?
85
PDB code
5my6
Structure name
crystal structure of a her2-nb complex
Structure deposition date
2017-01-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
544
Residue number B
560
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 544 of Receptor tyrosine-protein kinase erbB-2
Cysteine 560 of Receptor tyrosine-protein kinase erbB-2
3mzw A 202 A 213
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 224 and 235 (202 and 213 respectively in this structure).
Details
Redox score ?
85
PDB code
3mzw
Structure name
her2 extracelluar region with affinity matured 3-helix affibody zher2:342
Structure deposition date
2010-05-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
224
Residue number B
235
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 224 of Receptor tyrosine-protein kinase erbB-2
Cysteine 235 of Receptor tyrosine-protein kinase erbB-2
3mzw A 218 A 230
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 240 and 252 (218 and 230 respectively in this structure).
Details
Redox score ?
85
PDB code
3mzw
Structure name
her2 extracelluar region with affinity matured 3-helix affibody zher2:342
Structure deposition date
2010-05-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
240
Residue number B
252
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 240 of Receptor tyrosine-protein kinase erbB-2
Cysteine 252 of Receptor tyrosine-protein kinase erbB-2
1s78 A 214 A 222
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 236 and 244 (214 and 222 respectively in this structure).
Details
Redox score ?
84
PDB code
1s78
Structure name
insights into erbb signaling from the structure of the erbb2- pertuzumab complex
Structure deposition date
2004-01-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
236
Residue number B
244
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 236 of Receptor tyrosine-protein kinase erbB-2
Cysteine 244 of Receptor tyrosine-protein kinase erbB-2
1s78 B 489 B 498
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 511 and 520 (489 and 498 respectively in this structure).
Details
Redox score ?
83
PDB code
1s78
Structure name
insights into erbb signaling from the structure of the erbb2- pertuzumab complex
Structure deposition date
2004-01-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
511
Residue number B
520
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 511 of Receptor tyrosine-protein kinase erbB-2
Cysteine 520 of Receptor tyrosine-protein kinase erbB-2
5my6 A 26 A 53
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 26 and 53.
Details
Redox score ?
83
PDB code
5my6
Structure name
crystal structure of a her2-nb complex
Structure deposition date
2017-01-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
26
Residue number B
53
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 26 of Receptor tyrosine-protein kinase erbB-2
Cysteine 53 of Receptor tyrosine-protein kinase erbB-2
1s78 B 140 B 170
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 162 and 192 (140 and 170 respectively in this structure).
Details
Redox score ?
83
PDB code
1s78
Structure name
insights into erbb signaling from the structure of the erbb2- pertuzumab complex
Structure deposition date
2004-01-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
162
Residue number B
192
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 162 of Receptor tyrosine-protein kinase erbB-2
Cysteine 192 of Receptor tyrosine-protein kinase erbB-2
5kwg C 453 C 482
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 475 and 504 (453 and 482 respectively in this structure).
Details
Redox score ?
83
PDB code
5kwg
Structure name
crystal structure of extracellular domain of her2 in complex with fcab h10-03-6
Structure deposition date
2016-07-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
475
Residue number B
504
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 475 of Receptor tyrosine-protein kinase erbB-2
Cysteine 504 of Receptor tyrosine-protein kinase erbB-2
3wsq A 173 A 177
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 195 and 199 (173 and 177 respectively in this structure).
Details
Redox score ?
82
PDB code
3wsq
Structure name
structure of her2 with an fab
Structure deposition date
2014-03-20
Thiol separation (Å)
3
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
195
Residue number B
199
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 195 of Receptor tyrosine-protein kinase erbB-2
Cysteine 199 of Receptor tyrosine-protein kinase erbB-2
5kwg C 565 C 574
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 587 and 596 (565 and 574 respectively in this structure).
Details
Redox score ?
82
PDB code
5kwg
Structure name
crystal structure of extracellular domain of her2 in complex with fcab h10-03-6
Structure deposition date
2016-07-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
9
% buried
0
Peptide accession
P04626
Residue number A
587
Residue number B
596
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 587 of Receptor tyrosine-protein kinase erbB-2
Cysteine 596 of Receptor tyrosine-protein kinase erbB-2
5kwg C 541 C 554
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 563 and 576 (541 and 554 respectively in this structure).
Details
Redox score ?
82
PDB code
5kwg
Structure name
crystal structure of extracellular domain of her2 in complex with fcab h10-03-6
Structure deposition date
2016-07-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
5
% buried
52
Peptide accession
P04626
Residue number A
563
Residue number B
576
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 563 of Receptor tyrosine-protein kinase erbB-2
Cysteine 576 of Receptor tyrosine-protein kinase erbB-2
5o4g C 173 C 182
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 195 and 204 (173 and 182 respectively in this structure).
Details
Redox score ?
81
PDB code
5o4g
Structure name
her2 in complex with fab mf3958
Structure deposition date
2017-05-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
195
Residue number B
204
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 195 of Receptor tyrosine-protein kinase erbB-2
Cysteine 204 of Receptor tyrosine-protein kinase erbB-2
5kwg C 489 C 493
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 511 and 515 (489 and 493 respectively in this structure).
Details
Redox score ?
81
PDB code
5kwg
Structure name
crystal structure of extracellular domain of her2 in complex with fcab h10-03-6
Structure deposition date
2016-07-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
7
% buried
nan
Peptide accession
P04626
Residue number A
511
Residue number B
515
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 511 of Receptor tyrosine-protein kinase erbB-2
Cysteine 515 of Receptor tyrosine-protein kinase erbB-2
5kwg C 493 C 506
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 515 and 528 (493 and 506 respectively in this structure).
Details
Redox score ?
81
PDB code
5kwg
Structure name
crystal structure of extracellular domain of her2 in complex with fcab h10-03-6
Structure deposition date
2016-07-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
7
% buried
43
Peptide accession
P04626
Residue number A
515
Residue number B
528
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 515 of Receptor tyrosine-protein kinase erbB-2
Cysteine 528 of Receptor tyrosine-protein kinase erbB-2
6att A 230 A 242
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 252 and 264 (230 and 242 respectively in this structure).
Details
Redox score ?
78
PDB code
6att
Structure name
39s fab bound to her2 ecd
Structure deposition date
2017-08-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
252
Residue number B
264
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 252 of Receptor tyrosine-protein kinase erbB-2
Cysteine 264 of Receptor tyrosine-protein kinase erbB-2
5kwg C 198 C 205
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 220 and 227 (198 and 205 respectively in this structure).
Details
Redox score ?
76
PDB code
5kwg
Structure name
crystal structure of extracellular domain of her2 in complex with fcab h10-03-6
Structure deposition date
2016-07-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
9
% buried
25
Peptide accession
P04626
Residue number A
220
Residue number B
227
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 220 of Receptor tyrosine-protein kinase erbB-2
Cysteine 227 of Receptor tyrosine-protein kinase erbB-2
5my6 A 567 A 576
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 567 and 576.
Details
Redox score ?
76
PDB code
5my6
Structure name
crystal structure of a her2-nb complex
Structure deposition date
2017-01-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
567
Residue number B
576
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 567 of Receptor tyrosine-protein kinase erbB-2
Cysteine 576 of Receptor tyrosine-protein kinase erbB-2
3wsq A 202 A 205
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 224 and 227 (202 and 205 respectively in this structure).
Details
Redox score ?
76
PDB code
3wsq
Structure name
structure of her2 with an fab
Structure deposition date
2014-03-20
Thiol separation (Å)
3
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
224
Residue number B
227
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 224 of Receptor tyrosine-protein kinase erbB-2
Cysteine 227 of Receptor tyrosine-protein kinase erbB-2
3be1 A 506 A 518
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 528 and 540 (506 and 518 respectively in this structure).
Details
Redox score ?
75
PDB code
3be1
Structure name
dual specific bh1 fab in complex with the extracellular domain of her2/erbb-2
Structure deposition date
2007-11-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
528
Residue number B
540
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 528 of Receptor tyrosine-protein kinase erbB-2
Cysteine 540 of Receptor tyrosine-protein kinase erbB-2
6lbx B 584 B 596
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 584 and 596.
Details
Redox score ?
75
PDB code
6lbx
Structure name
crystal structure of her2 domain iv and rb-h2
Structure deposition date
2019-11-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
584
Residue number B
596
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 584 of Receptor tyrosine-protein kinase erbB-2
Cysteine 596 of Receptor tyrosine-protein kinase erbB-2
5kwg C 233 C 242
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 255 and 264 (233 and 242 respectively in this structure).
Details
Redox score ?
74
PDB code
5kwg
Structure name
crystal structure of extracellular domain of her2 in complex with fcab h10-03-6
Structure deposition date
2016-07-18
Thiol separation (Å)
5
Half-sphere exposure sum ?
74
Minimum pKa ?
6
% buried
48
Peptide accession
P04626
Residue number A
255
Residue number B
264
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 255 of Receptor tyrosine-protein kinase erbB-2
Cysteine 264 of Receptor tyrosine-protein kinase erbB-2
5my6 A 220 A 224
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 220 and 224.
Details
Redox score ?
74
PDB code
5my6
Structure name
crystal structure of a her2-nb complex
Structure deposition date
2017-01-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
220
Residue number B
224
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 220 of Receptor tyrosine-protein kinase erbB-2
Cysteine 224 of Receptor tyrosine-protein kinase erbB-2
5o4g C 218 C 222
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 240 and 244 (218 and 222 respectively in this structure).
Details
Redox score ?
74
PDB code
5o4g
Structure name
her2 in complex with fab mf3958
Structure deposition date
2017-05-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
240
Residue number B
244
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 240 of Receptor tyrosine-protein kinase erbB-2
Cysteine 244 of Receptor tyrosine-protein kinase erbB-2
5kwg C 218 C 242
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 240 and 264 (218 and 242 respectively in this structure).
Details
Redox score ?
74
PDB code
5kwg
Structure name
crystal structure of extracellular domain of her2 in complex with fcab h10-03-6
Structure deposition date
2016-07-18
Thiol separation (Å)
5
Half-sphere exposure sum ?
68
Minimum pKa ?
6
% buried
nan
Peptide accession
P04626
Residue number A
240
Residue number B
264
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 240 of Receptor tyrosine-protein kinase erbB-2
Cysteine 264 of Receptor tyrosine-protein kinase erbB-2
5my6 A 584 A 587
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 584 and 587.
Details
Redox score ?
73
PDB code
5my6
Structure name
crystal structure of a her2-nb complex
Structure deposition date
2017-01-25
Thiol separation (Å)
5
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
584
Residue number B
587
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 584 of Receptor tyrosine-protein kinase erbB-2
Cysteine 587 of Receptor tyrosine-protein kinase erbB-2
5kwg C 545 C 562
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 567 and 584 (545 and 562 respectively in this structure).
Details
Redox score ?
72
PDB code
5kwg
Structure name
crystal structure of extracellular domain of her2 in complex with fcab h10-03-6
Structure deposition date
2016-07-18
Thiol separation (Å)
5
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
26
Peptide accession
P04626
Residue number A
567
Residue number B
584
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 567 of Receptor tyrosine-protein kinase erbB-2
Cysteine 584 of Receptor tyrosine-protein kinase erbB-2
3h3b B 177 B 182
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 199 and 204 (177 and 182 respectively in this structure).
Details
Redox score ?
71
PDB code
3h3b
Structure name
crystal structure of the single-chain fv (scfv) fragment of an anti- erbb2 antibody cha21 in complex with residues 1-192 of erbb2 extracellular domain
Structure deposition date
2009-04-16
Thiol separation (Å)
5
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
199
Residue number B
204
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 199 of Receptor tyrosine-protein kinase erbB-2
Cysteine 204 of Receptor tyrosine-protein kinase erbB-2
2a91 A 494 A 499
A redox-regulated disulphide may form within Receptor tyrosine-protein kinase erbB-2 between cysteines 515 and 520 (494 and 499 respectively in this structure).
Details
Redox score ?
70
PDB code
2a91
Structure name
crystal structure of erbb2 domains 1-3
Structure deposition date
2005-07-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04626
Residue number A
515
Residue number B
520
Peptide name
Receptor tyrosine-protein kinase erbB-2
Ligandability
Cysteine 515 of Receptor tyrosine-protein kinase erbB-2
Cysteine 520 of Receptor tyrosine-protein kinase erbB-2
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