ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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D(3) dopamine receptor

Intermolecular
Cysteine 122 and cysteine 166
Intramolecular
Cysteine 355 and cysteine 358
Cysteine 103 and cysteine 181
Cysteine 102 and cysteine 103
Cysteine 102 and cysteine 181
A redox-regulated disulphide may form between two units of D(3) dopamine receptor at cysteines 122 and 166. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
3pbl
Structure name
structure of the human dopamine d3 receptor in complex with eticlopride
Structure deposition date
2010-10-20
Thiol separation (Å)
6
Half-sphere exposure sum ?
91
Minimum pKa ?
13
% buried
100
Peptide A name
D(3) dopamine receptor
Peptide B name
D(3) dopamine receptor
Peptide A accession
P35462
Peptide B accession
P35462
Peptide A residue number
122
Peptide B residue number
166

Ligandability

Cysteine 122 of D(3) dopamine 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 166 of D(3) dopamine 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 D(3) dopamine receptor between cysteines 355 and 358.

Details

Redox score ?
92
PDB code
3pbl
Structure name
structure of the human dopamine d3 receptor in complex with eticlopride
Structure deposition date
2010-10-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
30
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35462
Residue number A
355
Residue number B
358
Peptide name
D(3) dopamine receptor

Ligandability

Cysteine 355 of D(3) dopamine 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 358 of D(3) dopamine 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 D(3) dopamine receptor between cysteines 103 and 181.

Details

Redox score ?
83
PDB code
3pbl
Structure name
structure of the human dopamine d3 receptor in complex with eticlopride
Structure deposition date
2010-10-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35462
Residue number A
103
Residue number B
181
Peptide name
D(3) dopamine receptor

Ligandability

Cysteine 103 of D(3) dopamine 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 181 of D(3) dopamine 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 D(3) dopamine receptor between cysteines 102 and 103. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
3pbl
Structure name
structure of the human dopamine d3 receptor in complex with eticlopride
Structure deposition date
2010-10-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
nan
Peptide accession
P35462
Residue number A
102
Residue number B
103
Peptide name
D(3) dopamine receptor

Ligandability

Cysteine 102 of D(3) dopamine 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 103 of D(3) dopamine 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 D(3) dopamine receptor between cysteines 102 and 181. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
3pbl
Structure name
structure of the human dopamine d3 receptor in complex with eticlopride
Structure deposition date
2010-10-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
nan
Peptide accession
P35462
Residue number A
102
Residue number B
181
Peptide name
D(3) dopamine receptor

Ligandability

Cysteine 102 of D(3) dopamine 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 181 of D(3) dopamine 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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