a tool for identifying drug-targetable redox-active disulphides

Inhibitor of growth protein 2

Intramolecular

Cysteine 229 and cysteine 234

Cysteine 229 and cysteine 259

Cysteine 216 and cysteine 243

Cysteine 234 and cysteine 259

Cysteine 216 and cysteine 218

Cysteine 229 and cysteine 256

Cysteine 256 and cysteine 259

Cysteine 234 and cysteine 256

Cysteine 218 and cysteine 243

Cysteine 216 and cysteine 256

A redox-regulated disulphide may form within Inhibitor of growth protein 2 between cysteines 229 and 234.

Details

Redox score ?

87

PDB code

Structure name

crystal structure of ing2 phd finger in complex with h3k4me3 peptide

Structure deposition date

2006-02-24

Thiol separation (Å)

4

Half-sphere exposure sum ?

52

Minimum pK_a ?

7

% buried

16

Peptide accession

Residue number A

229

Residue number B

234

Peptide name

Inhibitor of growth protein 2

Ligandability

Cysteine 229 of Inhibitor of growth protein 2

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 234 of Inhibitor of growth protein 2

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 Inhibitor of growth protein 2 between cysteines 229 and 259.

Details

Redox score ?

86

PDB code

Structure name

crystal structure of ing2 phd finger in complex with h3k4me3 peptide

Structure deposition date

2006-02-24

Thiol separation (Å)

4

Half-sphere exposure sum ?

50

Minimum pK_a ?

7

% buried

8

Peptide accession

Residue number A

229

Residue number B

259

Peptide name

Inhibitor of growth protein 2

Ligandability

Cysteine 229 of Inhibitor of growth protein 2

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 259 of Inhibitor of growth protein 2

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 Inhibitor of growth protein 2 between cysteines 216 and 243.

Details

Redox score ?

86

PDB code

Structure name

crystal structure of ing2 phd finger in complex with h3k4me3 peptide

Structure deposition date

2006-02-24

Thiol separation (Å)

4

Half-sphere exposure sum ?

52

Minimum pK_a ?

6

% buried

17

Peptide accession

Residue number A

216

Residue number B

243

Peptide name

Inhibitor of growth protein 2

Ligandability

Cysteine 216 of Inhibitor of growth protein 2

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 243 of Inhibitor of growth protein 2

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 Inhibitor of growth protein 2 between cysteines 234 and 259.

Details

Redox score ?

85

PDB code

Structure name

crystal structure of ing2 phd finger in complex with h3k4me3 peptide

Structure deposition date

2006-02-24

Thiol separation (Å)

4

Half-sphere exposure sum ?

40

Minimum pK_a ?

8

% buried

8

Peptide accession

Residue number A

234

Residue number B

259

Peptide name

Inhibitor of growth protein 2

Ligandability

Cysteine 234 of Inhibitor of growth protein 2

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 259 of Inhibitor of growth protein 2

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 Inhibitor of growth protein 2 between cysteines 216 and 218.

Details

Redox score ?

84

PDB code

Structure name

crystal structure of ing2 phd finger in complex with h3k4me3 peptide

Structure deposition date

2006-02-24

Thiol separation (Å)

4

Half-sphere exposure sum ?

46

Minimum pK_a ?

6

% buried

14

Peptide accession

Residue number A

216

Residue number B

218

Peptide name

Inhibitor of growth protein 2

Ligandability

Cysteine 216 of Inhibitor of growth protein 2

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 218 of Inhibitor of growth protein 2

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 Inhibitor of growth protein 2 between cysteines 229 and 256.

Details

Redox score ?

84

PDB code

Structure name

crystal structure of ing2 phd finger in complex with h3k4me3 peptide

Structure deposition date

2006-02-24

Thiol separation (Å)

4

Half-sphere exposure sum ?

65

Minimum pK_a ?

7

% buried

18

Peptide accession

Residue number A

229

Residue number B

256

Peptide name

Inhibitor of growth protein 2

Ligandability

Cysteine 229 of Inhibitor of growth protein 2

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 256 of Inhibitor of growth protein 2

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 Inhibitor of growth protein 2 between cysteines 256 and 259.

Details

Redox score ?

83

PDB code

Structure name

crystal structure of ing2 phd finger in complex with h3k4me3 peptide

Structure deposition date

2006-02-24

Thiol separation (Å)

4

Half-sphere exposure sum ?

53

Minimum pK_a ?

8

% buried

9

Peptide accession

Residue number A

256

Residue number B

259

Peptide name

Inhibitor of growth protein 2

Ligandability

Cysteine 256 of Inhibitor of growth protein 2

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 259 of Inhibitor of growth protein 2

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 Inhibitor of growth protein 2 between cysteines 234 and 256.

Details

Redox score ?

81

PDB code

Structure name

crystal structure of ing2 phd finger in complex with h3k4me3 peptide

Structure deposition date

2006-02-24

Thiol separation (Å)

4

Half-sphere exposure sum ?

55

Minimum pK_a ?

9

% buried

17

Peptide accession

Residue number A

234

Residue number B

256

Peptide name

Inhibitor of growth protein 2

Ligandability

Cysteine 234 of Inhibitor of growth protein 2

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 256 of Inhibitor of growth protein 2

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 Inhibitor of growth protein 2 between cysteines 218 and 243.

Details

Redox score ?

79

PDB code

Structure name

crystal structure of ing2 phd finger in complex with h3k4me3 peptide

Structure deposition date

2006-02-24

Thiol separation (Å)

4

Half-sphere exposure sum ?

40

Minimum pK_a ?

9

% buried

2

Peptide accession

Residue number A

218

Residue number B

243

Peptide name

Inhibitor of growth protein 2

Ligandability

Cysteine 218 of Inhibitor of growth protein 2

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 243 of Inhibitor of growth protein 2

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 Inhibitor of growth protein 2 between cysteines 216 and 256. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

55

PDB code

Structure name

crystal structure of ing2 phd finger in complex with h3k4me3 peptide

Structure deposition date

2006-02-24

Thiol separation (Å)

9

Half-sphere exposure sum ?

63

Minimum pK_a ?

6

% buried

24

Peptide accession

Residue number A

216

Residue number B

256

Peptide name

Inhibitor of growth protein 2

Ligandability

Cysteine 216 of Inhibitor of growth protein 2

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 256 of Inhibitor of growth protein 2

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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