ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Alpha-2B adrenergic receptor

Intramolecular
Cysteine 85 and cysteine 96
Cysteine 85 and cysteine 164
Cysteine 397 and cysteine 401
Cysteine 383 and cysteine 417
Cysteine 104 and cysteine 185
A redox-regulated disulphide may form within Alpha-2B adrenergic receptor between cysteines 85 and 96 (85 and 164 respectively in this structure).

Details

Redox score ?
94
PDB code
6k41
Structure name
cryo-em structure of alpha2bar-goa complex
Structure deposition date
2019-05-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P18089
Residue number A
85
Residue number B
96
Peptide name
Alpha-2B adrenergic receptor

Ligandability

Cysteine 85 of Alpha-2B 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 96 of Alpha-2B 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 Alpha-2B adrenergic receptor between cysteines 85 and 164.

Details

Redox score ?
87
PDB code
6k42
Structure name
cryo-em structure of alpha2bar-gi1 complex
Structure deposition date
2019-05-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P18089
Residue number A
85
Residue number B
164
Peptide name
Alpha-2B adrenergic receptor

Ligandability

Cysteine 85 of Alpha-2B 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 164 of Alpha-2B 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 Alpha-2B adrenergic receptor between cysteines 397 and 401.

Details

Redox score ?
76
PDB code
6k42
Structure name
cryo-em structure of alpha2bar-gi1 complex
Structure deposition date
2019-05-23
Thiol separation (Å)
5
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
0
Peptide accession
P18089
Residue number A
397
Residue number B
401
Peptide name
Alpha-2B adrenergic receptor

Ligandability

Cysteine 397 of Alpha-2B 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 401 of Alpha-2B 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 Alpha-2B adrenergic receptor between cysteines 383 and 417. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
6k41
Structure name
cryo-em structure of alpha2bar-goa complex
Structure deposition date
2019-05-23
Thiol separation (Å)
6
Half-sphere exposure sum ?
60
Minimum pKa ?
11
% buried
62
Peptide accession
P18089
Residue number A
383
Residue number B
417
Peptide name
Alpha-2B adrenergic receptor

Ligandability

Cysteine 383 of Alpha-2B 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 417 of Alpha-2B 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 Alpha-2B adrenergic receptor between cysteines 104 and 185. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
6k41
Structure name
cryo-em structure of alpha2bar-goa complex
Structure deposition date
2019-05-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
62
Peptide accession
P18089
Residue number A
104
Residue number B
185
Peptide name
Alpha-2B adrenergic receptor

Ligandability

Cysteine 104 of Alpha-2B 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 185 of Alpha-2B 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.

If this tool was useful for finding a disulphide, please cite: