ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Histamine H2 receptor

Intramolecular
Cysteine 91 and cysteine 174
Cysteine 118 and cysteine 102
Cysteine 199 and cysteine 102
A redox-regulated disulphide may form within Histamine H2 receptor between cysteines 91 and 174.

Details

Redox score ?
90
PDB code
7ul3
Structure name
cryoem structure of inactive h2r bound to famotidine, nb6m, and nabfab
Structure deposition date
2022-04-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P25021
Residue number A
91
Residue number B
174
Peptide name
Histamine H2 receptor

Ligandability

Cysteine 91 of Histamine H2 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 174 of Histamine H2 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 H2 receptor between cysteines 118 and 102 (118 and 201 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
7ul3
Structure name
cryoem structure of inactive h2r bound to famotidine, nb6m, and nabfab
Structure deposition date
2022-04-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
52
Minimum pKa ?
10
% buried
22
Peptide accession
P25021
Residue number A
118
Residue number B
102
Peptide name
Histamine H2 receptor

Ligandability

Cysteine 118 of Histamine H2 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 102 of Histamine H2 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.

Uncertain whether structure cysteine 201 has been assigned to correct residue.
A redox-regulated disulphide may form within Histamine H2 receptor between cysteines 199 and 102 (199 and 201 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
7ul3
Structure name
cryoem structure of inactive h2r bound to famotidine, nb6m, and nabfab
Structure deposition date
2022-04-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
50
Minimum pKa ?
10
% buried
18
Peptide accession
P25021
Residue number A
199
Residue number B
102
Peptide name
Histamine H2 receptor

Ligandability

Cysteine 199 of Histamine H2 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 102 of Histamine H2 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.

Uncertain whether structure cysteine 201 has been assigned to correct residue.
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