a tool for identifying drug-targetable redox-active disulphides

Gasdermin-D

Intermolecular

Cysteine 299 and cysteine 299

Intramolecular

Cysteine 38 and cysteine 56

Cysteine 309 and cysteine 355

Cysteine 354 and cysteine 358

Cysteine 445 and cysteine 467

A redox-regulated disulphide may form between two units of Gasdermin-D at cysteines 299 and 299. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

60

PDB code

Structure name

crystal structure of the murine gasdermin d c-terminal domain

Structure deposition date

2017-08-15

Thiol separation (Å)

4

Half-sphere exposure sum ?

92

Minimum pK_a ?

11

% buried

100

Peptide A name

Gasdermin-D

Peptide B name

Gasdermin-D

Peptide A accession

Peptide B accession

Peptide A residue number

299

Peptide B residue number

299

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 Gasdermin-D between cysteines 38 and 56.

Details

Redox score ?

75

PDB code

Structure name

crystal structure of human gsdmd

Structure deposition date

2018-12-03

Thiol separation (Å)

5

Half-sphere exposure sum ?

63

Minimum pK_a ?

6

% buried

49

Peptide accession

Residue number A

38

Residue number B

56

Peptide name

Gasdermin-D

Ligandability

Cysteine 38 of Gasdermin-D

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 56 of Gasdermin-D

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 Gasdermin-D between cysteines 309 and 355. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

45

PDB code

Structure name

crystal structure of human gsdmd

Structure deposition date

2018-12-03

Thiol separation (Å)

9

Half-sphere exposure sum ?

57

Minimum pK_a ?

10

% buried

26

Peptide accession

Residue number A

309

Residue number B

355

Peptide name

Gasdermin-D

Ligandability

Cysteine 309 of Gasdermin-D

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 355 of Gasdermin-D

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 Gasdermin-D between cysteines 354 and 358. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

44

PDB code

Structure name

structure of caspase-1 in complex with gasdermin d

Structure deposition date

2020-01-13

Thiol separation (Å)

8

Half-sphere exposure sum ?

67

Minimum pK_a ?

10

% buried

34

Peptide accession

Residue number A

354

Residue number B

358

Peptide name

Gasdermin-D

Ligandability

Cysteine 354 of Gasdermin-D

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 Gasdermin-D

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 Gasdermin-D between cysteines 445 and 467. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

31

PDB code

Structure name

caspase-1 p20/p10 c285a in complex with human gsdmd-c domain

Structure deposition date

2019-08-02

Thiol separation (Å)

10

Half-sphere exposure sum ?

72

Minimum pK_a ?

11

% buried

72

Peptide accession

Residue number A

445

Residue number B

467

Peptide name

Gasdermin-D

Ligandability

Cysteine 445 of Gasdermin-D

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 467 of Gasdermin-D

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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