ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Cyclic nucleotide-gated cation channel beta-3

Intramolecular
Cysteine 233 and cysteine 234
Cysteine 234 and cysteine 369
Cysteine 369 and cysteine 397
A redox-regulated disulphide may form within Cyclic nucleotide-gated cation channel beta-3 between cysteines 233 and 234. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
7rhs
Structure name
cryo-em structure of apo-state of human cnga3/cngb3 channel
Structure deposition date
2021-07-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
63
Minimum pKa ?
11
% buried
66
Peptide accession
Q9NQW8
Residue number A
233
Residue number B
234
Peptide name
Cyclic nucleotide-gated cation channel beta-3

Ligandability

Cysteine 233 of Cyclic nucleotide-gated cation channel beta-3

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 Cyclic nucleotide-gated cation channel beta-3

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 Cyclic nucleotide-gated cation channel beta-3 between cysteines 234 and 369. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
7rhs
Structure name
cryo-em structure of apo-state of human cnga3/cngb3 channel
Structure deposition date
2021-07-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
66
Peptide accession
Q9NQW8
Residue number A
234
Residue number B
369
Peptide name
Cyclic nucleotide-gated cation channel beta-3

Ligandability

Cysteine 234 of Cyclic nucleotide-gated cation channel beta-3

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 369 of Cyclic nucleotide-gated cation channel beta-3

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 Cyclic nucleotide-gated cation channel beta-3 between cysteines 369 and 397. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
7rhs
Structure name
cryo-em structure of apo-state of human cnga3/cngb3 channel
Structure deposition date
2021-07-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
82
Peptide accession
Q9NQW8
Residue number A
369
Residue number B
397
Peptide name
Cyclic nucleotide-gated cation channel beta-3

Ligandability

Cysteine 369 of Cyclic nucleotide-gated cation channel beta-3

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 397 of Cyclic nucleotide-gated cation channel beta-3

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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