ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Beta-2 adrenergic receptor

Intramolecular
Cysteine 106 and cysteine 191
Cysteine 184 and cysteine 190
Cysteine 77 and cysteine 191
Cysteine 106 and cysteine 184
Cysteine 184 and cysteine 191
Cysteine 190 and cysteine 191
Cysteine 77 and cysteine 106
Cysteine 77 and cysteine 190
Cysteine 77 and cysteine 184
Cysteine 106 and cysteine 190
More...
Cysteine 327 and cysteine 341
Cysteine 77 and cysteine 116
Cysteine 15 and cysteine 341
Cysteine 226 and cysteine 2394
A redox-regulated disulphide may form within Beta-2 adrenergic receptor between cysteines 106 and 191.

Details

Redox score ?
76
PDB code
6ni3
Structure name
b2v2r-gs protein subcomplex of a gpcr-g protein-beta-arrestin mega- complex
Structure deposition date
2018-12-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
48
Peptide accession
P07550
Residue number A
106
Residue number B
191
Peptide name
Beta-2 adrenergic receptor

Ligandability

Cysteine 106 of Beta-2 adrenergic 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 191 of Beta-2 adrenergic 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 Beta-2 adrenergic receptor between cysteines 184 and 190.

Details

Redox score ?
76
PDB code
7dhi
Structure name
cryo-em structure of the partial agonist salbutamol-bound beta2 adrenergic receptor-gs protein complex
Structure deposition date
2020-11-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
9
% buried
0
Peptide accession
P07550
Residue number A
184
Residue number B
190
Peptide name
Beta-2 adrenergic receptor

Ligandability

Cysteine 184 of Beta-2 adrenergic 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 190 of Beta-2 adrenergic 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 Beta-2 adrenergic receptor between cysteines 77 and 191 (93 and 191 respectively in this structure).

Details

Redox score ?
60
PDB code
3pds
Structure name
irreversible agonist-beta2 adrenoceptor complex
Structure deposition date
2010-10-24
Thiol separation (Å)
6
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07550
Residue number A
77
Residue number B
191
Peptide name
Beta-2 adrenergic receptor

Ligandability

Cysteine 77 of Beta-2 adrenergic 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 191 of Beta-2 adrenergic 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 Beta-2 adrenergic receptor between cysteines 106 and 184. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
6ps6
Structure name
xfel beta2 ar structure by ligand exchange from timolol to timolol
Structure deposition date
2019-07-12
Thiol separation (Å)
7
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07550
Residue number A
106
Residue number B
184
Peptide name
Beta-2 adrenergic receptor

Ligandability

Cysteine 106 of Beta-2 adrenergic 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 184 of Beta-2 adrenergic 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 Beta-2 adrenergic receptor between cysteines 184 and 191. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
6ps5
Structure name
xfel beta2 ar structure by ligand exchange from timolol to propranolol
Structure deposition date
2019-07-12
Thiol separation (Å)
7
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07550
Residue number A
184
Residue number B
191
Peptide name
Beta-2 adrenergic receptor

Ligandability

Cysteine 184 of Beta-2 adrenergic 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 191 of Beta-2 adrenergic 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 Beta-2 adrenergic receptor between cysteines 190 and 191. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
6e67
Structure name
structure of beta2 adrenergic receptor fused to a gs peptide
Structure deposition date
2018-07-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07550
Residue number A
190
Residue number B
191
Peptide name
Beta-2 adrenergic receptor

Ligandability

Cysteine 190 of Beta-2 adrenergic 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 191 of Beta-2 adrenergic 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 Beta-2 adrenergic receptor between cysteines 77 and 106 (93 and 106 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
3pds
Structure name
irreversible agonist-beta2 adrenoceptor complex
Structure deposition date
2010-10-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07550
Residue number A
77
Residue number B
106
Peptide name
Beta-2 adrenergic receptor

Ligandability

Cysteine 77 of Beta-2 adrenergic 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 106 of Beta-2 adrenergic 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 Beta-2 adrenergic receptor between cysteines 77 and 190 (93 and 190 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
3pds
Structure name
irreversible agonist-beta2 adrenoceptor complex
Structure deposition date
2010-10-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07550
Residue number A
77
Residue number B
190
Peptide name
Beta-2 adrenergic receptor

Ligandability

Cysteine 77 of Beta-2 adrenergic 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 190 of Beta-2 adrenergic 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 Beta-2 adrenergic receptor between cysteines 77 and 184 (93 and 184 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
3pds
Structure name
irreversible agonist-beta2 adrenoceptor complex
Structure deposition date
2010-10-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07550
Residue number A
77
Residue number B
184
Peptide name
Beta-2 adrenergic receptor

Ligandability

Cysteine 77 of Beta-2 adrenergic 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 184 of Beta-2 adrenergic 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 Beta-2 adrenergic receptor between cysteines 106 and 190. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
6e67
Structure name
structure of beta2 adrenergic receptor fused to a gs peptide
Structure deposition date
2018-07-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07550
Residue number A
106
Residue number B
190
Peptide name
Beta-2 adrenergic receptor

Ligandability

Cysteine 106 of Beta-2 adrenergic 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 190 of Beta-2 adrenergic 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 Beta-2 adrenergic receptor between cysteines 327 and 341 (1327 and 1341 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
5jqh
Structure name
structure of beta2 adrenoceptor bound to carazolol and inactive-state stabilizing nanobody, nb60
Structure deposition date
2016-05-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
48
Peptide accession
P07550
Residue number A
327
Residue number B
341
Peptide name
Beta-2 adrenergic receptor

Ligandability

Cysteine 327 of Beta-2 adrenergic 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 341 of Beta-2 adrenergic 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 Beta-2 adrenergic receptor between cysteines 77 and 116. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
22
PDB code
6ps4
Structure name
xfel beta2 ar structure by ligand exchange from timolol to ici-118551
Structure deposition date
2019-07-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
80
Minimum pKa ?
13
% buried
94
Peptide accession
P07550
Residue number A
77
Residue number B
116
Peptide name
Beta-2 adrenergic receptor

Ligandability

Cysteine 77 of Beta-2 adrenergic 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 116 of Beta-2 adrenergic 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 Beta-2 adrenergic receptor between cysteines 15 and 341 (15 and 16 respectively in this structure).

Details

Redox score ?
nan
PDB code
1gq4
Structure name
structural determinants of the nherf interaction with beta2ar and pdgfr
Structure deposition date
2001-11-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
57
Minimum pKa ?
9
% buried
19
Peptide accession
P07550
Residue number A
15
Residue number B
341
Peptide name
Beta-2 adrenergic receptor

Ligandability

Cysteine 15 of Beta-2 adrenergic 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 341 of Beta-2 adrenergic 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 15 in protein A could not be asigned to a Uniprot residue.
Uncertain whether structure cysteine 16 has been assigned to correct residue.
A redox-regulated disulphide may form within Beta-2 adrenergic receptor between cysteines 226 and 2394.

Details

Redox score ?
nan
PDB code
6e67
Structure name
structure of beta2 adrenergic receptor fused to a gs peptide
Structure deposition date
2018-07-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07550
Residue number A
226
Residue number B
2394
Peptide name
Beta-2 adrenergic receptor

Ligandability

Cysteine 226 of Beta-2 adrenergic 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 2394 of Beta-2 adrenergic 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 226 in protein A could not be asigned to a Uniprot residue.
Cysteine 2394 in protein B could not be asigned to a Uniprot residue.
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