a tool for identifying drug-targetable redox-active disulphides

Potassium voltage-gated channel subfamily B member 1

Intermolecular

Cysteine 111 and cysteine 133

Cysteine 111 and cysteine 132

Intramolecular

Cysteine 132 and cysteine 133

Cysteine 63 and cysteine 73

A redox-regulated disulphide may form between two units of Potassium voltage-gated channel subfamily B member 1 at cysteines 111 and 133.

Details

Redox score ?

94

PDB code

Structure name

crystal structure of the tetramerization domain (29-147) from human voltage-gated potassium channel kv2

Structure deposition date

2021-07-12

Thiol separation (Å)

3

Half-sphere exposure sum ?

nan

Minimum pK_a ?

7

% buried

14

Peptide A name

Potassium voltage-gated channel subfamily B member 1

Peptide B name

Potassium voltage-gated channel subfamily B member 1

Peptide A accession

Peptide B accession

Peptide A residue number

111

Peptide B residue number

133

Ligandability

Cysteine 111 of Potassium voltage-gated channel subfamily B member 1

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 133 of Potassium voltage-gated channel subfamily B member 1

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 between two units of Potassium voltage-gated channel subfamily B member 1 at cysteines 111 and 132.

Details

Redox score ?

80

PDB code

Structure name

crystal structure of the tetramerization domain (29-147) from human voltage-gated potassium channel kv2

Structure deposition date

2021-07-12

Thiol separation (Å)

4

Half-sphere exposure sum ?

40

Minimum pK_a ?

9

% buried

8

Peptide A name

Potassium voltage-gated channel subfamily B member 1

Peptide B name

Potassium voltage-gated channel subfamily B member 1

Peptide A accession

Peptide B accession

Peptide A residue number

111

Peptide B residue number

132

Ligandability

Cysteine 111 of Potassium voltage-gated channel subfamily B member 1

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 132 of Potassium voltage-gated channel subfamily B member 1

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 Potassium voltage-gated channel subfamily B member 1 between cysteines 132 and 133.

Details

Redox score ?

81

PDB code

Structure name

crystal structure of the tetramerization domain (29-147) from human voltage-gated potassium channel kv2

Structure deposition date

2021-07-12

Thiol separation (Å)

4

Half-sphere exposure sum ?

39

Minimum pK_a ?

8

% buried

11

Peptide accession

Residue number A

132

Residue number B

133

Peptide name

Potassium voltage-gated channel subfamily B member 1

Ligandability

Cysteine 132 of Potassium voltage-gated channel subfamily B member 1

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 133 of Potassium voltage-gated channel subfamily B member 1

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 Potassium voltage-gated channel subfamily B member 1 between cysteines 63 and 73. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

59

PDB code

Structure name

crystal structure of the tetramerization domain (29-147) from human voltage-gated potassium channel kv2

Structure deposition date

2021-11-02

Thiol separation (Å)

7

Half-sphere exposure sum ?

52

Minimum pK_a ?

10

% buried

42

Peptide accession

Residue number A

63

Residue number B

73

Peptide name

Potassium voltage-gated channel subfamily B member 1

Ligandability

Cysteine 63 of Potassium voltage-gated channel subfamily B member 1

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 73 of Potassium voltage-gated channel subfamily B member 1

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.

If this tool was useful for finding a disulphide, please cite: