ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Nociceptin receptor

Intramolecular
Cysteine 123 and cysteine 200
Cysteine 153 and cysteine 234
Cysteine 275 and cysteine 313
Cysteine 62 and cysteine 70
Cysteine 62 and cysteine 313
A redox-regulated disulphide may form within Nociceptin receptor between cysteines 123 and 200.

Details

Redox score ?
85
PDB code
4ea3
Structure name
structure of the n/ofq opioid receptor in complex with a peptide mimetic
Structure deposition date
2012-03-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P41146
Residue number A
123
Residue number B
200
Peptide name
Nociceptin receptor

Ligandability

Cysteine 123 of Nociceptin 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 200 of Nociceptin 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 Nociceptin receptor between cysteines 153 and 234. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
5dhg
Structure name
the crystal structure of nociceptin/orphanin fq peptide receptor (nop) in complex with c-35 (psi community target)
Structure deposition date
2015-08-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
16
Peptide accession
P41146
Residue number A
153
Residue number B
234
Peptide name
Nociceptin receptor

Ligandability

Cysteine 153 of Nociceptin 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 234 of Nociceptin 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 Nociceptin receptor between cysteines 275 and 313. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
4ea3
Structure name
structure of the n/ofq opioid receptor in complex with a peptide mimetic
Structure deposition date
2012-03-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
60
Peptide accession
P41146
Residue number A
275
Residue number B
313
Peptide name
Nociceptin receptor

Ligandability

Cysteine 275 of Nociceptin 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 313 of Nociceptin 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 Nociceptin receptor between cysteines 62 and 70. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
4ea3
Structure name
structure of the n/ofq opioid receptor in complex with a peptide mimetic
Structure deposition date
2012-03-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
10
% buried
52
Peptide accession
P41146
Residue number A
62
Residue number B
70
Peptide name
Nociceptin receptor

Ligandability

Cysteine 62 of Nociceptin 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 70 of Nociceptin 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 Nociceptin receptor between cysteines 62 and 313. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
5dhh
Structure name
the crystal structure of nociceptin/orphanin fq peptide receptor (nop) in complex with sb-612111 (psi community target)
Structure deposition date
2015-08-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
11
% buried
76
Peptide accession
P41146
Residue number A
62
Residue number B
313
Peptide name
Nociceptin receptor

Ligandability

Cysteine 62 of Nociceptin 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 313 of Nociceptin 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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