a tool for identifying drug-targetable redox-active disulphides

Follistatin-related protein 1

Intramolecular

Cysteine 34 and cysteine 50

Cysteine 29 and cysteine 40

Cysteine 56 and cysteine 75

Cysteine 64 and cysteine 96

Cysteine 52 and cysteine 82

Cysteine 34 and cysteine 40

Cysteine 40 and cysteine 50

Cysteine 29 and cysteine 34

Cysteine 29 and cysteine 50

Cysteine 50 and cysteine 82

Cysteine 34 and cysteine 82

Cysteine 75 and cysteine 82

A redox-regulated disulphide may form within Follistatin-related protein 1 between cysteines 34 and 50.

Details

Redox score ?

88

PDB code

Structure name

structure of fstl1

Structure deposition date

2019-04-30

Thiol separation (Å)

2

Half-sphere exposure sum ?

45

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

34

Residue number B

50

Peptide name

Follistatin-related protein 1

Ligandability

Cysteine 34 of Follistatin-related protein 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 50 of Follistatin-related protein 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 Follistatin-related protein 1 between cysteines 29 and 40.

Details

Redox score ?

87

PDB code

Structure name

structure of fstl1

Structure deposition date

2019-04-30

Thiol separation (Å)

2

Half-sphere exposure sum ?

48

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

29

Residue number B

40

Peptide name

Follistatin-related protein 1

Ligandability

Cysteine 29 of Follistatin-related protein 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 40 of Follistatin-related protein 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 Follistatin-related protein 1 between cysteines 56 and 75.

Details

Redox score ?

86

PDB code

Structure name

structure of fstl1

Structure deposition date

2019-04-30

Thiol separation (Å)

2

Half-sphere exposure sum ?

56

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

56

Residue number B

75

Peptide name

Follistatin-related protein 1

Ligandability

Cysteine 56 of Follistatin-related protein 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 75 of Follistatin-related protein 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 Follistatin-related protein 1 between cysteines 64 and 96.

Details

Redox score ?

85

PDB code

Structure name

structure of fstl1

Structure deposition date

2019-04-30

Thiol separation (Å)

2

Half-sphere exposure sum ?

46

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

64

Residue number B

96

Peptide name

Follistatin-related protein 1

Ligandability

Cysteine 64 of Follistatin-related protein 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 96 of Follistatin-related protein 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 Follistatin-related protein 1 between cysteines 52 and 82.

Details

Redox score ?

84

PDB code

Structure name

structure of fstl1

Structure deposition date

2019-04-30

Thiol separation (Å)

2

Half-sphere exposure sum ?

51

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

52

Residue number B

82

Peptide name

Follistatin-related protein 1

Ligandability

Cysteine 52 of Follistatin-related protein 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 82 of Follistatin-related protein 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 Follistatin-related protein 1 between cysteines 34 and 40.

Details

Redox score ?

72

PDB code

Structure name

structure of fstl1

Structure deposition date

2019-04-30

Thiol separation (Å)

5

Half-sphere exposure sum ?

49

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

34

Residue number B

40

Peptide name

Follistatin-related protein 1

Ligandability

Cysteine 34 of Follistatin-related protein 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 40 of Follistatin-related protein 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 Follistatin-related protein 1 between cysteines 40 and 50.

Details

Redox score ?

64

PDB code

Structure name

structure of fstl1

Structure deposition date

2019-04-30

Thiol separation (Å)

6

Half-sphere exposure sum ?

50

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

40

Residue number B

50

Peptide name

Follistatin-related protein 1

Ligandability

Cysteine 40 of Follistatin-related protein 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 50 of Follistatin-related protein 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 Follistatin-related protein 1 between cysteines 29 and 34.

Details

Redox score ?

63

PDB code

Structure name

structure of fstl1

Structure deposition date

2019-04-30

Thiol separation (Å)

7

Half-sphere exposure sum ?

41

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

29

Residue number B

34

Peptide name

Follistatin-related protein 1

Ligandability

Cysteine 29 of Follistatin-related protein 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 34 of Follistatin-related protein 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 Follistatin-related protein 1 between cysteines 29 and 50. 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

structure of fstl1

Structure deposition date

2019-04-30

Thiol separation (Å)

8

Half-sphere exposure sum ?

43

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

29

Residue number B

50

Peptide name

Follistatin-related protein 1

Ligandability

Cysteine 29 of Follistatin-related protein 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 50 of Follistatin-related protein 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 Follistatin-related protein 1 between cysteines 50 and 82. 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 fstl1

Structure deposition date

2019-04-30

Thiol separation (Å)

9

Half-sphere exposure sum ?

48

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

50

Residue number B

82

Peptide name

Follistatin-related protein 1

Ligandability

Cysteine 50 of Follistatin-related protein 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 82 of Follistatin-related protein 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 Follistatin-related protein 1 between cysteines 34 and 82. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

43

PDB code

Structure name

structure of fstl1

Structure deposition date

2019-04-30

Thiol separation (Å)

10

Half-sphere exposure sum ?

47

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

34

Residue number B

82

Peptide name

Follistatin-related protein 1

Ligandability

Cysteine 34 of Follistatin-related protein 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 82 of Follistatin-related protein 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 Follistatin-related protein 1 between cysteines 75 and 82. 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

structure of fstl1

Structure deposition date

2019-04-30

Thiol separation (Å)

10

Half-sphere exposure sum ?

58

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

75

Residue number B

82

Peptide name

Follistatin-related protein 1

Ligandability

Cysteine 75 of Follistatin-related protein 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 82 of Follistatin-related protein 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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