ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Adhesion G protein-coupled receptor B1

Intermolecular
Cysteine 461 and cysteine 446
Intramolecular
Cysteine 436 and cysteine 446
Cysteine 425 and cysteine 461
Cysteine 421 and cysteine 456
Cysteine 421 and cysteine 461
Cysteine 421 and cysteine 425
A redox-regulated disulphide may form between two units of Adhesion G protein-coupled receptor B1 at cysteines 461 and 446 (53 and 38 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
7r84
Structure name
structure of mouse bai1 (adgrb1) tsr3 domain in p21 space group
Structure deposition date
2021-06-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
32
Minimum pKa ?
nan
% buried
nan
Peptide A name
Adhesion G protein-coupled receptor B1
Peptide B name
Adhesion G protein-coupled receptor B1
Peptide A accession
Q3UHD1
Peptide B accession
Q3UHD1
Peptide A residue number
461
Peptide B residue number
446

Ligandability

Cysteine 461 of Adhesion G protein-coupled receptor B1

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 446 of Adhesion G protein-coupled receptor B1

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 Adhesion G protein-coupled receptor B1 between cysteines 436 and 446 (28 and 38 respectively in this structure).

Details

Redox score ?
91
PDB code
7r86
Structure name
structure of mouse bai1 (adgrb1) in complex with mouse nogo receptor (rtn4r)
Structure deposition date
2021-06-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3UHD1
Residue number A
436
Residue number B
446
Peptide name
Adhesion G protein-coupled receptor B1

Ligandability

Cysteine 436 of Adhesion G protein-coupled receptor B1

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 446 of Adhesion G protein-coupled receptor B1

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 Adhesion G protein-coupled receptor B1 between cysteines 425 and 461 (17 and 53 respectively in this structure).

Details

Redox score ?
87
PDB code
7r84
Structure name
structure of mouse bai1 (adgrb1) tsr3 domain in p21 space group
Structure deposition date
2021-06-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
33
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3UHD1
Residue number A
425
Residue number B
461
Peptide name
Adhesion G protein-coupled receptor B1

Ligandability

Cysteine 425 of Adhesion G protein-coupled receptor B1

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 461 of Adhesion G protein-coupled receptor B1

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 Adhesion G protein-coupled receptor B1 between cysteines 421 and 456 (13 and 48 respectively in this structure).

Details

Redox score ?
86
PDB code
7r86
Structure name
structure of mouse bai1 (adgrb1) in complex with mouse nogo receptor (rtn4r)
Structure deposition date
2021-06-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3UHD1
Residue number A
421
Residue number B
456
Peptide name
Adhesion G protein-coupled receptor B1

Ligandability

Cysteine 421 of Adhesion G protein-coupled receptor B1

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 456 of Adhesion G protein-coupled receptor B1

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 Adhesion G protein-coupled receptor B1 between cysteines 421 and 461 (13 and 53 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
7r84
Structure name
structure of mouse bai1 (adgrb1) tsr3 domain in p21 space group
Structure deposition date
2021-06-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
36
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3UHD1
Residue number A
421
Residue number B
461
Peptide name
Adhesion G protein-coupled receptor B1

Ligandability

Cysteine 421 of Adhesion G protein-coupled receptor B1

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 461 of Adhesion G protein-coupled receptor B1

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 Adhesion G protein-coupled receptor B1 between cysteines 421 and 425 (13 and 17 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
7r86
Structure name
structure of mouse bai1 (adgrb1) in complex with mouse nogo receptor (rtn4r)
Structure deposition date
2021-06-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3UHD1
Residue number A
421
Residue number B
425
Peptide name
Adhesion G protein-coupled receptor B1

Ligandability

Cysteine 421 of Adhesion G protein-coupled receptor B1

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 425 of Adhesion G protein-coupled receptor B1

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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