a tool for identifying drug-targetable redox-active disulphides

Pannexin-1

Intermolecular

Cysteine 426 and cysteine 426

Intramolecular

Cysteine 66 and cysteine 265

Cysteine 84 and cysteine 246

Cysteine 66 and cysteine 84

Cysteine 66 and cysteine 246

Cysteine 84 and cysteine 264

Cysteine 246 and cysteine 265

A redox-regulated disulphide may form between two units of Pannexin-1 at cysteines 426 and 426 (434 and 434 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

54

PDB code

Structure name

human pannexin1 model

Structure deposition date

2021-01-17

Thiol separation (Å)

8

Half-sphere exposure sum ?

nan

Minimum pK_a ?

13

% buried

67

Peptide A name

Pannexin-1

Peptide B name

Pannexin-1

Peptide A accession

Peptide B accession

Peptide A residue number

426

Peptide B residue number

426

Ligandability

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 Pannexin-1 between cysteines 66 and 265.

Details

Redox score ?

80

PDB code

Structure name

the cryo-em structure of human pannexin 1

Structure deposition date

2020-03-13

Thiol separation (Å)

2

Half-sphere exposure sum ?

86

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

66

Residue number B

265

Peptide name

Pannexin-1

Ligandability

Cysteine 66 of Pannexin-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 265 of Pannexin-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 Pannexin-1 between cysteines 84 and 246.

Details

Redox score ?

78

PDB code

Structure name

cryo-em structure of c-terminal truncated human pannexin1

Structure deposition date

2020-01-23

Thiol separation (Å)

4

Half-sphere exposure sum ?

73

Minimum pK_a ?

7

% buried

78

Peptide accession

Residue number A

84

Residue number B

246

Peptide name

Pannexin-1

Ligandability

Cysteine 84 of Pannexin-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 246 of Pannexin-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 Pannexin-1 between cysteines 66 and 84.

Details

Redox score ?

76

PDB code

Structure name

cryo-em structure of mouse pannexin 1 purified in salipro nanoparticles

Structure deposition date

2022-06-07

Thiol separation (Å)

4

Half-sphere exposure sum ?

87

Minimum pK_a ?

5

% buried

100

Peptide accession

Residue number A

66

Residue number B

84

Peptide name

Pannexin-1

Ligandability

Cysteine 66 of Pannexin-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 84 of Pannexin-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 Pannexin-1 between cysteines 66 and 246.

Details

Redox score ?

73

PDB code

Structure name

cryo-em structure of human pannexin 1 channel with its c-terminal tail cleaved by caspase-7, in complex with cbx

Structure deposition date

2020-03-26

Thiol separation (Å)

3

Half-sphere exposure sum ?

86

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

66

Residue number B

246

Peptide name

Pannexin-1

Ligandability

Cysteine 66 of Pannexin-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 246 of Pannexin-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 Pannexin-1 between cysteines 84 and 264.

Details

Redox score ?

63

PDB code

Structure name

cryo-em structure of mouse pannexin 1 purified in salipro nanoparticles

Structure deposition date

2022-06-07

Thiol separation (Å)

3

Half-sphere exposure sum ?

90

Minimum pK_a ?

12

% buried

100

Peptide accession

Residue number A

84

Residue number B

264

Peptide name

Pannexin-1

Ligandability

Cysteine 84 of Pannexin-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 264 of Pannexin-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 Pannexin-1 between cysteines 246 and 265. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

48

PDB code

Structure name

cryo-em structure of human pannexin 1 channel with its c-terminal tail cleaved by caspase-7, in complex with cbx

Structure deposition date

2020-03-26

Thiol separation (Å)

7

Half-sphere exposure sum ?

90

Minimum pK_a ?

11

% buried

nan

Peptide accession

Residue number A

246

Residue number B

265

Peptide name

Pannexin-1

Ligandability

Cysteine 246 of Pannexin-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 265 of Pannexin-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.

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