ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Histamine H3 receptor

Intramolecular
Cysteine 107 and cysteine 188
Cysteine 384 and cysteine 388
Cysteine 87 and cysteine 118
A redox-regulated disulphide may form within Histamine H3 receptor between cysteines 107 and 188.

Details

Redox score ?
84
PDB code
7f61
Structure name
crystal structure of human histamine receptor h3r in complex with antagonist pf03654746
Structure deposition date
2021-06-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y5N1
Residue number A
107
Residue number B
188
Peptide name
Histamine H3 receptor

Ligandability

Cysteine 107 of Histamine H3 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 188 of Histamine H3 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 Histamine H3 receptor between cysteines 384 and 388.

Details

Redox score ?
83
PDB code
7f61
Structure name
crystal structure of human histamine receptor h3r in complex with antagonist pf03654746
Structure deposition date
2021-06-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
35
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y5N1
Residue number A
384
Residue number B
388
Peptide name
Histamine H3 receptor

Ligandability

Cysteine 384 of Histamine H3 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 388 of Histamine H3 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 Histamine H3 receptor between cysteines 87 and 118. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
21
PDB code
7f61
Structure name
crystal structure of human histamine receptor h3r in complex with antagonist pf03654746
Structure deposition date
2021-06-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
14
% buried
100
Peptide accession
Q9Y5N1
Residue number A
87
Residue number B
118
Peptide name
Histamine H3 receptor

Ligandability

Cysteine 87 of Histamine H3 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 118 of Histamine H3 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.

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