ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Beta-1 adrenergic receptor

Intramolecular
Cysteine 209 and cysteine 215
Cysteine 141 and cysteine 24
A redox-regulated disulphide may form within Beta-1 adrenergic receptor between cysteines 209 and 215 (13 and 19 respectively in this structure).

Details

Redox score ?
88
PDB code
2lsq
Structure name
analog of the fragment 197-221 of beta-1 adrenoreceptor
Structure deposition date
2012-05-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
34
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08588
Residue number A
209
Residue number B
215
Peptide name
Beta-1 adrenergic receptor

Ligandability

Cysteine 209 of Beta-1 adrenergic receptor

Cysteine 215 of Beta-1 adrenergic receptor

A redox-regulated disulphide may form within Beta-1 adrenergic receptor between cysteines 141 and 24 (2 and 24 respectively in this structure).

Details

Redox score ?
nan
PDB code
2lsq
Structure name
analog of the fragment 197-221 of beta-1 adrenoreceptor
Structure deposition date
2012-05-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
27
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08588
Residue number A
141
Residue number B
24
Peptide name
Beta-1 adrenergic receptor

Ligandability

Cysteine 141 of Beta-1 adrenergic receptor

Cysteine 24 of Beta-1 adrenergic receptor

Cysteine 24 in protein B could not be asigned to a Uniprot residue.
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