ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Orexin receptor type 2

Intramolecular
Cysteine 127 and cysteine 210
Cysteine 127 and cysteine 193
Cysteine 193 and cysteine 210
Cysteine 181 and cysteine 1188
Cysteine 1004 and cysteine 181
A redox-regulated disulphide may form within Orexin receptor type 2 between cysteines 127 and 210.

Details

Redox score ?
85
PDB code
6tpg
Structure name
crystal structure of the orexin-2 receptor in complex with empa at 2
Structure deposition date
2019-12-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q548Y0
Residue number A
127
Residue number B
210
Peptide name
Orexin receptor type 2

Ligandability

Cysteine 127 of Orexin receptor type 2

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 210 of Orexin receptor type 2

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 Orexin receptor type 2 between cysteines 127 and 193.

Details

Redox score ?
73
PDB code
6tpj
Structure name
crystal structure of the orexin-2 receptor in complex with suvorexant at 2
Structure deposition date
2019-12-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
nan
Peptide accession
Q548Y0
Residue number A
127
Residue number B
193
Peptide name
Orexin receptor type 2

Ligandability

Cysteine 127 of Orexin receptor type 2

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 193 of Orexin receptor type 2

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 Orexin receptor type 2 between cysteines 193 and 210.

Details

Redox score ?
61
PDB code
6tpj
Structure name
crystal structure of the orexin-2 receptor in complex with suvorexant at 2
Structure deposition date
2019-12-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
57
Minimum pKa ?
9
% buried
nan
Peptide accession
Q548Y0
Residue number A
193
Residue number B
210
Peptide name
Orexin receptor type 2

Ligandability

Cysteine 193 of Orexin receptor type 2

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 210 of Orexin receptor type 2

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 Orexin receptor type 2 between cysteines 181 and 1188 (1133 and 1188 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
6tpj
Structure name
crystal structure of the orexin-2 receptor in complex with suvorexant at 2
Structure deposition date
2019-12-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
80
Peptide accession
Q548Y0
Residue number A
181
Residue number B
1188
Peptide name
Orexin receptor type 2

Ligandability

Cysteine 181 of Orexin receptor type 2

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 1188 of Orexin receptor type 2

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 1188 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Orexin receptor type 2 between cysteines 1004 and 181 (1004 and 1133 respectively in this structure).

Details

Redox score ?
nan
PDB code
6tpj
Structure name
crystal structure of the orexin-2 receptor in complex with suvorexant at 2
Structure deposition date
2019-12-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
65
Minimum pKa ?
9
% buried
54
Peptide accession
Q548Y0
Residue number A
1004
Residue number B
181
Peptide name
Orexin receptor type 2

Ligandability

Cysteine 1004 of Orexin receptor type 2

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 181 of Orexin receptor type 2

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 1004 in protein A could not be asigned to a Uniprot residue.
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