a tool for identifying drug-targetable redox-active disulphides

E3 ubiquitin-protein ligase SHPRH

Intramolecular

Cysteine 677 and cysteine 706

Cysteine 677 and cysteine 680 L

Cysteine 677 and cysteine 703

Cysteine 661 and cysteine 663

Cysteine 661 and cysteine 688

Cysteine 703 and cysteine 706

Cysteine 680 and cysteine 703 L

Cysteine 680 and cysteine 706 L

Cysteine 663 and cysteine 688

Cysteine 1229 and cysteine 1241

Cysteine 1241 and cysteine 1244

Cysteine 1229 and cysteine 1244

Cysteine 1229 and cysteine 1240

Cysteine 1012 and cysteine 1016

Cysteine 1240 and cysteine 1241

Cysteine 1240 and cysteine 1244

Cysteine 661 and cysteine 703

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase SHPRH between cysteines 677 and 706.

Details

Redox score ?

86

PDB code

Structure name

phd domain from human shprh

Structure deposition date

2013-05-07

Thiol separation (Å)

4

Half-sphere exposure sum ?

44

Minimum pK_a ?

7

% buried

8

Peptide accession

Residue number A

677

Residue number B

706

Peptide name

E3 ubiquitin-protein ligase SHPRH

Ligandability

Cysteine 677 of E3 ubiquitin-protein ligase SHPRH

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 706 of E3 ubiquitin-protein ligase SHPRH

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 E3 ubiquitin-protein ligase SHPRH between cysteines 677 and 680.

Details

Redox score ?

86

PDB code

Structure name

phd domain from human shprh

Structure deposition date

2013-05-07

Thiol separation (Å)

4

Half-sphere exposure sum ?

48

Minimum pK_a ?

7

% buried

10

Peptide accession

Residue number A

677

Residue number B

680

Peptide name

E3 ubiquitin-protein ligase SHPRH

Ligandability

Cysteine 677 of E3 ubiquitin-protein ligase SHPRH

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 680 of E3 ubiquitin-protein ligase SHPRH

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.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase SHPRH between cysteines 677 and 703.

Details

Redox score ?

85

PDB code

Structure name

phd domain from human shprh

Structure deposition date

2013-05-07

Thiol separation (Å)

4

Half-sphere exposure sum ?

57

Minimum pK_a ?

7

% buried

16

Peptide accession

Residue number A

677

Residue number B

703

Peptide name

E3 ubiquitin-protein ligase SHPRH

Ligandability

Cysteine 677 of E3 ubiquitin-protein ligase SHPRH

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 703 of E3 ubiquitin-protein ligase SHPRH

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 E3 ubiquitin-protein ligase SHPRH between cysteines 661 and 663.

Details

Redox score ?

85

PDB code

Structure name

phd domain from human shprh

Structure deposition date

2013-05-07

Thiol separation (Å)

4

Half-sphere exposure sum ?

45

Minimum pK_a ?

7

% buried

8

Peptide accession

Residue number A

661

Residue number B

663

Peptide name

E3 ubiquitin-protein ligase SHPRH

Ligandability

Cysteine 661 of E3 ubiquitin-protein ligase SHPRH

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 663 of E3 ubiquitin-protein ligase SHPRH

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 E3 ubiquitin-protein ligase SHPRH between cysteines 661 and 688.

Details

Redox score ?

83

PDB code

Structure name

phd domain from human shprh

Structure deposition date

2013-05-07

Thiol separation (Å)

4

Half-sphere exposure sum ?

55

Minimum pK_a ?

7

% buried

9

Peptide accession

Residue number A

661

Residue number B

688

Peptide name

E3 ubiquitin-protein ligase SHPRH

Ligandability

Cysteine 661 of E3 ubiquitin-protein ligase SHPRH

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 688 of E3 ubiquitin-protein ligase SHPRH

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 E3 ubiquitin-protein ligase SHPRH between cysteines 703 and 706.

Details

Redox score ?

82

PDB code

Structure name

phd domain from human shprh

Structure deposition date

2013-05-07

Thiol separation (Å)

4

Half-sphere exposure sum ?

51

Minimum pK_a ?

8

% buried

8

Peptide accession

Residue number A

703

Residue number B

706

Peptide name

E3 ubiquitin-protein ligase SHPRH

Ligandability

Cysteine 703 of E3 ubiquitin-protein ligase SHPRH

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 706 of E3 ubiquitin-protein ligase SHPRH

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 E3 ubiquitin-protein ligase SHPRH between cysteines 680 and 703.

Details

Redox score ?

81

PDB code

Structure name

phd domain from human shprh

Structure deposition date

2013-05-07

Thiol separation (Å)

4

Half-sphere exposure sum ?

55

Minimum pK_a ?

8

% buried

9

Peptide accession

Residue number A

680

Residue number B

703

Peptide name

E3 ubiquitin-protein ligase SHPRH

Ligandability

Cysteine 680 of E3 ubiquitin-protein ligase SHPRH

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 703 of E3 ubiquitin-protein ligase SHPRH

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 E3 ubiquitin-protein ligase SHPRH between cysteines 680 and 706.

Details

Redox score ?

77

PDB code

Structure name

phd domain from human shprh

Structure deposition date

2013-05-07

Thiol separation (Å)

4

Half-sphere exposure sum ?

42

Minimum pK_a ?

10

% buried

2

Peptide accession

Residue number A

680

Residue number B

706

Peptide name

E3 ubiquitin-protein ligase SHPRH

Ligandability

Cysteine 680 of E3 ubiquitin-protein ligase SHPRH

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 706 of E3 ubiquitin-protein ligase SHPRH

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 E3 ubiquitin-protein ligase SHPRH between cysteines 663 and 688.

Details

Redox score ?

76

PDB code

Structure name

phd domain from human shprh

Structure deposition date

2013-05-07

Thiol separation (Å)

4

Half-sphere exposure sum ?

42

Minimum pK_a ?

10

% buried

2

Peptide accession

Residue number A

663

Residue number B

688

Peptide name

E3 ubiquitin-protein ligase SHPRH

Ligandability

Cysteine 663 of E3 ubiquitin-protein ligase SHPRH

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 688 of E3 ubiquitin-protein ligase SHPRH

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 E3 ubiquitin-protein ligase SHPRH between cysteines 1229 and 1241.

Details

Redox score ?

75

PDB code

Structure name

crystal structure of a functionally uncharacterized domain of e3 ubiquitin ligase shprh

Structure deposition date

2014-06-17

Thiol separation (Å)

4

Half-sphere exposure sum ?

50

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1229

Residue number B

1241

Peptide name

E3 ubiquitin-protein ligase SHPRH

Ligandability

Cysteine 1229 of E3 ubiquitin-protein ligase SHPRH

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 1241 of E3 ubiquitin-protein ligase SHPRH

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 E3 ubiquitin-protein ligase SHPRH between cysteines 1241 and 1244.

Details

Redox score ?

74

PDB code

Structure name

crystal structure of a functionally uncharacterized domain of e3 ubiquitin ligase shprh

Structure deposition date

2014-06-17

Thiol separation (Å)

4

Half-sphere exposure sum ?

52

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1241

Residue number B

1244

Peptide name

E3 ubiquitin-protein ligase SHPRH

Ligandability

Cysteine 1241 of E3 ubiquitin-protein ligase SHPRH

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 1244 of E3 ubiquitin-protein ligase SHPRH

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 E3 ubiquitin-protein ligase SHPRH between cysteines 1229 and 1244.

Details

Redox score ?

74

PDB code

Structure name

crystal structure of a functionally uncharacterized domain of e3 ubiquitin ligase shprh

Structure deposition date

2014-06-17

Thiol separation (Å)

4

Half-sphere exposure sum ?

51

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1229

Residue number B

1244

Peptide name

E3 ubiquitin-protein ligase SHPRH

Ligandability

Cysteine 1229 of E3 ubiquitin-protein ligase SHPRH

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 1244 of E3 ubiquitin-protein ligase SHPRH

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 E3 ubiquitin-protein ligase SHPRH between cysteines 1229 and 1240.

Details

Redox score ?

68

PDB code

Structure name

crystal structure of a functionally uncharacterized domain of e3 ubiquitin ligase shprh

Structure deposition date

2014-06-17

Thiol separation (Å)

4

Half-sphere exposure sum ?

45

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1229

Residue number B

1240

Peptide name

E3 ubiquitin-protein ligase SHPRH

Ligandability

Cysteine 1229 of E3 ubiquitin-protein ligase SHPRH

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 1240 of E3 ubiquitin-protein ligase SHPRH

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 E3 ubiquitin-protein ligase SHPRH between cysteines 1012 and 1016.

Details

Redox score ?

68

PDB code

Structure name

crystal structure of a functionally uncharacterized domain of e3 ubiquitin ligase shprh

Structure deposition date

2014-06-17

Thiol separation (Å)

5

Half-sphere exposure sum ?

63

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1012

Residue number B

1016

Peptide name

E3 ubiquitin-protein ligase SHPRH

Ligandability

Cysteine 1012 of E3 ubiquitin-protein ligase SHPRH

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 1016 of E3 ubiquitin-protein ligase SHPRH

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 E3 ubiquitin-protein ligase SHPRH between cysteines 1240 and 1241. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

57

PDB code

Structure name

crystal structure of a functionally uncharacterized domain of e3 ubiquitin ligase shprh

Structure deposition date

2014-06-17

Thiol separation (Å)

7

Half-sphere exposure sum ?

45

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1240

Residue number B

1241

Peptide name

E3 ubiquitin-protein ligase SHPRH

Ligandability

Cysteine 1240 of E3 ubiquitin-protein ligase SHPRH

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 1241 of E3 ubiquitin-protein ligase SHPRH

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 E3 ubiquitin-protein ligase SHPRH between cysteines 1240 and 1244. 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

crystal structure of a functionally uncharacterized domain of e3 ubiquitin ligase shprh

Structure deposition date

2014-06-17

Thiol separation (Å)

7

Half-sphere exposure sum ?

45

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1240

Residue number B

1244

Peptide name

E3 ubiquitin-protein ligase SHPRH

Ligandability

Cysteine 1240 of E3 ubiquitin-protein ligase SHPRH

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 1244 of E3 ubiquitin-protein ligase SHPRH

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 E3 ubiquitin-protein ligase SHPRH between cysteines 661 and 703. 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

phd domain from human shprh

Structure deposition date

2013-05-07

Thiol separation (Å)

10

Half-sphere exposure sum ?

61

Minimum pK_a ?

7

% buried

15

Peptide accession

Residue number A

661

Residue number B

703

Peptide name

E3 ubiquitin-protein ligase SHPRH

Ligandability

Cysteine 661 of E3 ubiquitin-protein ligase SHPRH

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 703 of E3 ubiquitin-protein ligase SHPRH

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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