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a tool for identifying drug-targetable redox-active disulphides

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Epidermal growth factor receptor

Intramolecular
Cysteine 157 and cysteine 240
Cysteine 526 and cysteine 511
Cysteine 329 and cysteine 333
Cysteine 624 and cysteine 636
Cysteine 311 and cysteine 326 L
Cysteine 595 and cysteine 617
Cysteine 620 and cysteine 628
Cysteine 558 and cysteine 571
Cysteine 194 and cysteine 207 L
Cysteine 562 and cysteine 579
More...
Cysteine 526 and cysteine 535
Cysteine 264 and cysteine 291
Cysteine 215 and cysteine 223
Cysteine 582 and cysteine 591
Cysteine 539 and cysteine 555
Cysteine 219 and cysteine 231 L
Cysteine 31 and cysteine 362
Cysteine 236 and cysteine 248 L
Cysteine 295 and cysteine 307
Cysteine 190 and cysteine 199
Cysteine 251 and cysteine 260 L
Cysteine 232 and cysteine 240
Cysteine 31 and cysteine 58
Cysteine 506 and cysteine 515
Cysteine 337 and cysteine 362
Cysteine 470 and cysteine 499
Cysteine 510 and cysteine 523
Cysteine 157 and cysteine 187
Cysteine 248 and cysteine 260 L
Cysteine 190 and cysteine 194
Cysteine 579 and cysteine 591
Cysteine 510 and cysteine 515
Cysteine 523 and cysteine 535
Cysteine 571 and cysteine 579
Cysteine 523 and cysteine 511
Cysteine 620 and cysteine 624
Cysteine 624 and cysteine 628
Cysteine 194 and cysteine 199
Cysteine 215 and cysteine 219
Cysteine 562 and cysteine 571
A redox-regulated disulphide may form within Epidermal growth factor receptor between cysteines 157 and 240 (208 and 216 respectively in this structure).

Details

Redox score ?
92
PDB code
4krp
Structure name
nanobody/vhh domain 9g8 in complex with the extracellular region of egfr
Structure deposition date
2013-05-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
157
Residue number B
240
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 157 of Epidermal growth factor receptor

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 240 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 526 and 511 (502 and 511 respectively in this structure).

Details

Redox score ?
92
PDB code
4krm
Structure name
nanobody/vhh domain 7d12 in complex with domain iii of the extracellular region of egfr, ph 3
Structure deposition date
2013-05-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
526
Residue number B
511
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 526 of Epidermal growth factor receptor

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 511 of Epidermal growth factor receptor

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 511 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Epidermal growth factor receptor between cysteines 329 and 333 (305 and 309 respectively in this structure).

Details

Redox score ?
91
PDB code
5wb7
Structure name
crystal structure of the epidermal growth factor receptor extracellular region in complex with epiregulin
Structure deposition date
2017-06-28
Thiol separation (Å)
2
Half-sphere exposure sum ?
34
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
329
Residue number B
333
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 329 of Epidermal growth factor receptor

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 333 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 624 and 636 (600 and 612 respectively in this structure).

Details

Redox score ?
89
PDB code
3njp
Structure name
the extracellular and transmembrane domain interfaces in epidermal growth factor receptor signaling
Structure deposition date
2010-06-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
624
Residue number B
636
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 624 of Epidermal growth factor receptor

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 636 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 311 and 326 (287 and 302 respectively in this structure).

Details

Redox score ?
88
PDB code
6aru
Structure name
structure of cetuximab fab mutant in complex with egfr extracellular domain
Structure deposition date
2017-08-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
311
Residue number B
326
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 311 of Epidermal growth factor receptor

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 326 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 595 and 617 (571 and 593 respectively in this structure).

Details

Redox score ?
87
PDB code
6aru
Structure name
structure of cetuximab fab mutant in complex with egfr extracellular domain
Structure deposition date
2017-08-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
595
Residue number B
617
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 595 of Epidermal growth factor receptor

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 617 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 620 and 628 (596 and 604 respectively in this structure).

Details

Redox score ?
86
PDB code
3njp
Structure name
the extracellular and transmembrane domain interfaces in epidermal growth factor receptor signaling
Structure deposition date
2010-06-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
620
Residue number B
628
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 620 of Epidermal growth factor receptor

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 628 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 558 and 571 (534 and 547 respectively in this structure).

Details

Redox score ?
86
PDB code
4krp
Structure name
nanobody/vhh domain 9g8 in complex with the extracellular region of egfr
Structure deposition date
2013-05-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
558
Residue number B
571
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 558 of Epidermal growth factor receptor

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 571 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 194 and 207 (170 and 183 respectively in this structure).

Details

Redox score ?
86
PDB code
1ivo
Structure name
crystal structure of the complex of human epidermal growth factor and receptor extracellular domains
Structure deposition date
2002-03-28
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
194
Residue number B
207
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 194 of Epidermal growth factor receptor

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 207 of Epidermal growth factor receptor

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Epidermal growth factor receptor between cysteines 562 and 579 (538 and 555 respectively in this structure).

Details

Redox score ?
86
PDB code
7om4
Structure name
nanobody egb4 bound to the full extracellular egfr-egf complex
Structure deposition date
2021-05-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
562
Residue number B
579
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 562 of Epidermal growth factor receptor

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 579 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 526 and 535 (502 and 511 respectively in this structure).

Details

Redox score ?
85
PDB code
4krp
Structure name
nanobody/vhh domain 9g8 in complex with the extracellular region of egfr
Structure deposition date
2013-05-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
526
Residue number B
535
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 526 of Epidermal growth factor receptor

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 535 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 264 and 291 (240 and 267 respectively in this structure).

Details

Redox score ?
85
PDB code
4krp
Structure name
nanobody/vhh domain 9g8 in complex with the extracellular region of egfr
Structure deposition date
2013-05-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
264
Residue number B
291
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 264 of Epidermal growth factor receptor

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 291 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 215 and 223 (191 and 199 respectively in this structure).

Details

Redox score ?
85
PDB code
7lfs
Structure name
crystal structure of the epidermal growth factor receptor extracellular region with a265v mutation in complex with epiregulin
Structure deposition date
2021-01-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
215
Residue number B
223
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 215 of Epidermal growth factor receptor

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 223 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 582 and 591 (558 and 567 respectively in this structure).

Details

Redox score ?
85
PDB code
6aru
Structure name
structure of cetuximab fab mutant in complex with egfr extracellular domain
Structure deposition date
2017-08-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
582
Residue number B
591
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 582 of Epidermal growth factor receptor

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 591 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 539 and 555 (515 and 531 respectively in this structure).

Details

Redox score ?
85
PDB code
4uv7
Structure name
the complex structure of extracellular domain of egfr and gc1118a
Structure deposition date
2014-08-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
539
Residue number B
555
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 539 of Epidermal growth factor receptor

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 555 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 219 and 231 (195 and 207 respectively in this structure).

Details

Redox score ?
84
PDB code
6aru
Structure name
structure of cetuximab fab mutant in complex with egfr extracellular domain
Structure deposition date
2017-08-23
Thiol separation (Å)
3
Half-sphere exposure sum ?
58
Minimum pKa ?
8
% buried
2
Peptide accession
P00533
Residue number A
219
Residue number B
231
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 219 of Epidermal growth factor receptor

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 231 of Epidermal growth factor receptor

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Epidermal growth factor receptor between cysteines 31 and 362 (313 and 338 respectively in this structure).

Details

Redox score ?
84
PDB code
5sx4
Structure name
crystal structure of panitumumab in complex with epidermal growth factor receptor domain 3
Structure deposition date
2016-08-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
31
Residue number B
362
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 31 of Epidermal growth factor receptor

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 362 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 236 and 248 (212 and 224 respectively in this structure).

Details

Redox score ?
84
PDB code
7len
Structure name
crystal structure of the epidermal growth factor receptor extracellular region with r84k mutation in complex with epiregulin crystallized with trehalose
Structure deposition date
2021-01-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
236
Residue number B
248
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 236 of Epidermal growth factor receptor

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 248 of Epidermal growth factor receptor

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Epidermal growth factor receptor between cysteines 295 and 307 (271 and 283 respectively in this structure).

Details

Redox score ?
84
PDB code
1mox
Structure name
crystal structure of human epidermal growth factor receptor (residues 1-501) in complex with tgf-alpha
Structure deposition date
2002-09-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
295
Residue number B
307
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 295 of Epidermal growth factor receptor

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 307 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 190 and 199 (166 and 175 respectively in this structure).

Details

Redox score ?
83
PDB code
7lfs
Structure name
crystal structure of the epidermal growth factor receptor extracellular region with a265v mutation in complex with epiregulin
Structure deposition date
2021-01-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
190
Residue number B
199
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 190 of Epidermal growth factor receptor

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 199 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 251 and 260 (227 and 236 respectively in this structure).

Details

Redox score ?
83
PDB code
4kro
Structure name
nanobody/vhh domain ega1 in complex with the extracellular region of egfr
Structure deposition date
2013-05-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
251
Residue number B
260
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 251 of Epidermal growth factor receptor

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 260 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 232 and 240 (208 and 216 respectively in this structure).

Details

Redox score ?
83
PDB code
5wb7
Structure name
crystal structure of the epidermal growth factor receptor extracellular region in complex with epiregulin
Structure deposition date
2017-06-28
Thiol separation (Å)
2
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
232
Residue number B
240
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 232 of Epidermal growth factor receptor

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 240 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 31 and 58 (7 and 34 respectively in this structure).

Details

Redox score ?
83
PDB code
7lfs
Structure name
crystal structure of the epidermal growth factor receptor extracellular region with a265v mutation in complex with epiregulin
Structure deposition date
2021-01-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
31
Residue number B
58
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 31 of Epidermal growth factor receptor

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 58 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 506 and 515 (482 and 491 respectively in this structure).

Details

Redox score ?
83
PDB code
3c09
Structure name
crystal structure the fab fragment of matuzumab (fab72000) in complex with domain iii of the extracellular region of egfr
Structure deposition date
2008-01-18
Thiol separation (Å)
3
Half-sphere exposure sum ?
67
Minimum pKa ?
8
% buried
6
Peptide accession
P00533
Residue number A
506
Residue number B
515
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 506 of Epidermal growth factor receptor

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 515 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 337 and 362 (313 and 338 respectively in this structure).

Details

Redox score ?
82
PDB code
3qwq
Structure name
crystal structure of the extracellular domain of the epidermal growth factor receptor in complex with an adnectin
Structure deposition date
2011-02-28
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
337
Residue number B
362
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 337 of Epidermal growth factor receptor

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 362 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 470 and 499 (446 and 475 respectively in this structure).

Details

Redox score ?
81
PDB code
1mox
Structure name
crystal structure of human epidermal growth factor receptor (residues 1-501) in complex with tgf-alpha
Structure deposition date
2002-09-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
470
Residue number B
499
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 470 of Epidermal growth factor receptor

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 499 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 510 and 523 (486 and 499 respectively in this structure).

Details

Redox score ?
80
PDB code
5sx5
Structure name
crystal structure of panitumumab in complex with epidermal growth factor receptor domain 3 mutant s468r
Structure deposition date
2016-08-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
14
Peptide accession
P00533
Residue number A
510
Residue number B
523
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 510 of Epidermal growth factor receptor

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 523 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 157 and 187 (133 and 163 respectively in this structure).

Details

Redox score ?
80
PDB code
4uip
Structure name
the complex structure of extracellular domain of egfr with repebody (rac1)
Structure deposition date
2015-03-31
Thiol separation (Å)
3
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
30
Peptide accession
P00533
Residue number A
157
Residue number B
187
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 157 of Epidermal growth factor receptor

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 187 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 248 and 260 (224 and 236 respectively in this structure).

Details

Redox score ?
78
PDB code
5wb8
Structure name
crystal structure of the epidermal growth factor receptor extracellular region in complex with epigen
Structure deposition date
2017-06-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
248
Residue number B
260
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 248 of Epidermal growth factor receptor

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 260 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 190 and 194 (166 and 170 respectively in this structure).

Details

Redox score ?
77
PDB code
1ivo
Structure name
crystal structure of the complex of human epidermal growth factor and receptor extracellular domains
Structure deposition date
2002-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
190
Residue number B
194
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 190 of Epidermal growth factor receptor

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 194 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 579 and 591 (555 and 567 respectively in this structure).

Details

Redox score ?
77
PDB code
4uv7
Structure name
the complex structure of extracellular domain of egfr and gc1118a
Structure deposition date
2014-08-05
Thiol separation (Å)
3
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
579
Residue number B
591
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 579 of Epidermal growth factor receptor

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 591 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 510 and 515 (486 and 491 respectively in this structure).

Details

Redox score ?
77
PDB code
5wb8
Structure name
crystal structure of the epidermal growth factor receptor extracellular region in complex with epigen
Structure deposition date
2017-06-28
Thiol separation (Å)
3
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
510
Residue number B
515
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 510 of Epidermal growth factor receptor

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 515 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 523 and 535 (499 and 511 respectively in this structure).

Details

Redox score ?
75
PDB code
4krp
Structure name
nanobody/vhh domain 9g8 in complex with the extracellular region of egfr
Structure deposition date
2013-05-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
523
Residue number B
535
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 523 of Epidermal growth factor receptor

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 535 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 571 and 579 (547 and 555 respectively in this structure).

Details

Redox score ?
75
PDB code
4uip
Structure name
the complex structure of extracellular domain of egfr with repebody (rac1)
Structure deposition date
2015-03-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
571
Residue number B
579
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 571 of Epidermal growth factor receptor

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 579 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 523 and 511 (499 and 511 respectively in this structure).

Details

Redox score ?
74
PDB code
4krm
Structure name
nanobody/vhh domain 7d12 in complex with domain iii of the extracellular region of egfr, ph 3
Structure deposition date
2013-05-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
523
Residue number B
511
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 523 of Epidermal growth factor receptor

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 511 of Epidermal growth factor receptor

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 511 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Epidermal growth factor receptor between cysteines 620 and 624 (596 and 600 respectively in this structure).

Details

Redox score ?
74
PDB code
4kro
Structure name
nanobody/vhh domain ega1 in complex with the extracellular region of egfr
Structure deposition date
2013-05-16
Thiol separation (Å)
5
Half-sphere exposure sum ?
39
Minimum pKa ?
9
% buried
nan
Peptide accession
P00533
Residue number A
620
Residue number B
624
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 620 of Epidermal growth factor receptor

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 624 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 624 and 628 (600 and 604 respectively in this structure).

Details

Redox score ?
73
PDB code
3njp
Structure name
the extracellular and transmembrane domain interfaces in epidermal growth factor receptor signaling
Structure deposition date
2010-06-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
624
Residue number B
628
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 624 of Epidermal growth factor receptor

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 628 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 194 and 199 (170 and 175 respectively in this structure).

Details

Redox score ?
73
PDB code
5wb7
Structure name
crystal structure of the epidermal growth factor receptor extracellular region in complex with epiregulin
Structure deposition date
2017-06-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
194
Residue number B
199
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 194 of Epidermal growth factor receptor

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 199 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 215 and 219 (191 and 195 respectively in this structure).

Details

Redox score ?
73
PDB code
7lfs
Structure name
crystal structure of the epidermal growth factor receptor extracellular region with a265v mutation in complex with epiregulin
Structure deposition date
2021-01-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
215
Residue number B
219
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 215 of Epidermal growth factor receptor

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 219 of Epidermal growth factor receptor

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 Epidermal growth factor receptor between cysteines 562 and 571 (538 and 547 respectively in this structure).

Details

Redox score ?
72
PDB code
3b2v
Structure name
crystal structure of the extracellular region of the epidermal growth factor receptor in complex with the fab fragment of imc-11f8
Structure deposition date
2007-10-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00533
Residue number A
562
Residue number B
571
Peptide name
Epidermal growth factor receptor

Ligandability

Cysteine 562 of Epidermal growth factor receptor

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 571 of Epidermal growth factor receptor

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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