ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Orexin/Hypocretin receptor type 1

Intramolecular
Cysteine 119 and cysteine 202
Cysteine 119 and cysteine 185
Cysteine 185 and cysteine 202
Cysteine 99 and cysteine 202
Cysteine 1004 and cysteine 99
A redox-regulated disulphide may form within Orexin/Hypocretin receptor type 1 between cysteines 119 and 202.

Details

Redox score ?
86
PDB code
6tq6
Structure name
crystal structure of the orexin-1 receptor in complex with compound 14
Structure deposition date
2019-12-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43613
Residue number A
119
Residue number B
202
Peptide name
Orexin/Hypocretin receptor type 1

Ligandability

Cysteine 119 of Orexin/Hypocretin receptor type 1

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 202 of Orexin/Hypocretin receptor type 1

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/Hypocretin receptor type 1 between cysteines 119 and 185.

Details

Redox score ?
69
PDB code
6tp4
Structure name
crystal structure of the orexin-1 receptor in complex with act-462206
Structure deposition date
2019-12-12
Thiol separation (Å)
5
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
nan
Peptide accession
O43613
Residue number A
119
Residue number B
185
Peptide name
Orexin/Hypocretin receptor type 1

Ligandability

Cysteine 119 of Orexin/Hypocretin receptor type 1

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 Orexin/Hypocretin receptor type 1

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/Hypocretin receptor type 1 between cysteines 185 and 202.

Details

Redox score ?
64
PDB code
6tot
Structure name
crystal structure of the orexin-1 receptor in complex with lemborexant
Structure deposition date
2019-12-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
nan
Peptide accession
O43613
Residue number A
185
Residue number B
202
Peptide name
Orexin/Hypocretin receptor type 1

Ligandability

Cysteine 185 of Orexin/Hypocretin receptor type 1

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 202 of Orexin/Hypocretin receptor type 1

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/Hypocretin receptor type 1 between cysteines 99 and 202 (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 ?
31
PDB code
6v9s
Structure name
structure-based development of subtype-selective orexin 1 receptor antagonists
Structure deposition date
2019-12-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
76
Peptide accession
O43613
Residue number A
99
Residue number B
202
Peptide name
Orexin/Hypocretin receptor type 1

Ligandability

Cysteine 99 of Orexin/Hypocretin receptor type 1

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 202 of Orexin/Hypocretin receptor type 1

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.

Uncertain whether structure cysteine 1188 has been assigned to correct residue.
A redox-regulated disulphide may form within Orexin/Hypocretin receptor type 1 between cysteines 1004 and 99 (1004 and 1133 respectively in this structure).

Details

Redox score ?
nan
PDB code
6v9s
Structure name
structure-based development of subtype-selective orexin 1 receptor antagonists
Structure deposition date
2019-12-16
Thiol separation (Å)
5
Half-sphere exposure sum ?
65
Minimum pKa ?
9
% buried
48
Peptide accession
O43613
Residue number A
1004
Residue number B
99
Peptide name
Orexin/Hypocretin receptor type 1

Ligandability

Cysteine 1004 of Orexin/Hypocretin receptor type 1

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 99 of Orexin/Hypocretin receptor type 1

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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