ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Orexin receptor type 2

Intramolecular
Cysteine 381 and cysteine 382
Cysteine 127 and cysteine 210
Cysteine 382 and cysteine 383
Cysteine 127 and cysteine 193
Cysteine 193 and cysteine 210
Cysteine 381 and cysteine 383
Cysteine 157 and cysteine 252
Cysteine 181 and cysteine 1188
Cysteine 1004 and cysteine 181
A redox-regulated disulphide may form within Orexin receptor type 2 between cysteines 381 and 382.

Details

Redox score ?
86
PDB code
5wqc
Structure name
crystal structure of human orexin 2 receptor bound to the selective antagonist empa determined by the synchrotron light source at spring- 8
Structure deposition date
2016-11-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
17
Minimum pKa ?
9
% buried
0
Peptide accession
O43614
Residue number A
381
Residue number B
382
Peptide name
Orexin receptor type 2

Ligandability

Cysteine 381 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 382 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 210.

Details

Redox score ?
85
PDB code
6tpn
Structure name
crystal structure of the orexin-2 receptor in complex with htl6641 at 2
Structure deposition date
2019-12-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43614
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 382 and 383.

Details

Redox score ?
72
PDB code
5wqc
Structure name
crystal structure of human orexin 2 receptor bound to the selective antagonist empa determined by the synchrotron light source at spring- 8
Structure deposition date
2016-11-25
Thiol separation (Å)
6
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
0
Peptide accession
O43614
Residue number A
382
Residue number B
383
Peptide name
Orexin receptor type 2

Ligandability

Cysteine 382 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 383 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 ?
72
PDB code
5ws3
Structure name
crystal structures of human orexin 2 receptor bound to the selective antagonist empa determined by serial femtosecond crystallography at sacla
Structure deposition date
2016-12-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
nan
Peptide accession
O43614
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 ?
67
PDB code
4s0v
Structure name
crystal structure of the human ox2 orexin receptor bound to the insomnia drug suvorexant
Structure deposition date
2015-01-06
Thiol separation (Å)
5
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
nan
Peptide accession
O43614
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 381 and 383.

Details

Redox score ?
62
PDB code
5wqc
Structure name
crystal structure of human orexin 2 receptor bound to the selective antagonist empa determined by the synchrotron light source at spring- 8
Structure deposition date
2016-11-25
Thiol separation (Å)
8
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
0
Peptide accession
O43614
Residue number A
381
Residue number B
383
Peptide name
Orexin receptor type 2

Ligandability

Cysteine 381 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 383 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 157 and 252. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
7sqo
Structure name
structure of the orexin-2 receptor(ox2r) bound to tak-925, gi and scfv16
Structure deposition date
2021-11-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
48
Minimum pKa ?
9
% buried
18
Peptide accession
O43614
Residue number A
157
Residue number B
252
Peptide name
Orexin receptor type 2

Ligandability

Cysteine 157 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 252 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).

Details

Redox score ?
nan
PDB code
6tpn
Structure name
crystal structure of the orexin-2 receptor in complex with htl6641 at 2
Structure deposition date
2019-12-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
78
Peptide accession
O43614
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
5wqc
Structure name
crystal structure of human orexin 2 receptor bound to the selective antagonist empa determined by the synchrotron light source at spring- 8
Structure deposition date
2016-11-25
Thiol separation (Å)
5
Half-sphere exposure sum ?
70
Minimum pKa ?
9
% buried
58
Peptide accession
O43614
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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