a tool for identifying drug-targetable redox-active disulphides

Cysteine protease ATG4A

Intramolecular

Cysteine 117 and cysteine 125

Cysteine 77 and cysteine 81 L

Cysteine 117 and cysteine 124

Cysteine 124 and cysteine 125

Cysteine 324 and cysteine 334

Cysteine 186 and cysteine 324

A redox-regulated disulphide may form within Cysteine protease ATG4A between cysteines 117 and 125.

Details

Redox score ?

69

PDB code

Structure name

cysteine protease atg4a

Structure deposition date

2007-03-21

Thiol separation (Å)

4

Half-sphere exposure sum ?

72

Minimum pK_a ?

8

% buried

76

Peptide accession

Residue number A

117

Residue number B

125

Peptide name

Cysteine protease ATG4A

Ligandability

Cysteine 117 of Cysteine protease ATG4A

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 125 of Cysteine protease ATG4A

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 Cysteine protease ATG4A between cysteines 77 and 81. 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

cysteine protease atg4a

Structure deposition date

2007-03-21

Thiol separation (Å)

6

Half-sphere exposure sum ?

92

Minimum pK_a ?

8

% buried

86

Peptide accession

Residue number A

77

Residue number B

81

Peptide name

Cysteine protease ATG4A

Ligandability

Cysteine 77 of Cysteine protease ATG4A

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 81 of Cysteine protease ATG4A

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 Cysteine protease ATG4A between cysteines 117 and 124. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

51

PDB code

Structure name

cysteine protease atg4a

Structure deposition date

2007-03-21

Thiol separation (Å)

7

Half-sphere exposure sum ?

59

Minimum pK_a ?

10

% buried

71

Peptide accession

Residue number A

117

Residue number B

124

Peptide name

Cysteine protease ATG4A

Ligandability

Cysteine 117 of Cysteine protease ATG4A

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 124 of Cysteine protease ATG4A

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 Cysteine protease ATG4A between cysteines 124 and 125. 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

cysteine protease atg4a

Structure deposition date

2007-03-21

Thiol separation (Å)

7

Half-sphere exposure sum ?

58

Minimum pK_a ?

12

% buried

64

Peptide accession

Residue number A

124

Residue number B

125

Peptide name

Cysteine protease ATG4A

Ligandability

Cysteine 124 of Cysteine protease ATG4A

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 125 of Cysteine protease ATG4A

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 Cysteine protease ATG4A between cysteines 324 and 334. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

41

PDB code

Structure name

cysteine protease atg4a

Structure deposition date

2007-03-21

Thiol separation (Å)

7

Half-sphere exposure sum ?

69

Minimum pK_a ?

12

% buried

84

Peptide accession

Residue number A

324

Residue number B

334

Peptide name

Cysteine protease ATG4A

Ligandability

Cysteine 324 of Cysteine protease ATG4A

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 334 of Cysteine protease ATG4A

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 Cysteine protease ATG4A between cysteines 186 and 324. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

37

PDB code

Structure name

cysteine protease atg4a

Structure deposition date

2007-03-21

Thiol separation (Å)

8

Half-sphere exposure sum ?

72

Minimum pK_a ?

13

% buried

94

Peptide accession

Residue number A

186

Residue number B

324

Peptide name

Cysteine protease ATG4A

Ligandability

Cysteine 186 of Cysteine protease ATG4A

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 324 of Cysteine protease ATG4A

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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