a tool for identifying drug-targetable redox-active disulphides

PHD finger protein 13

Intramolecular

Cysteine 249 and cysteine 277

Cysteine 249 and cysteine 252

Cysteine 249 and cysteine 274

Cysteine 252 and cysteine 277

Cysteine 252 and cysteine 274

Cysteine 235 and cysteine 237

Cysteine 274 and cysteine 277

Cysteine 237 and cysteine 260

Cysteine 235 and cysteine 260

Cysteine 235 and cysteine 274

Cysteine 235 and cysteine 252

A redox-regulated disulphide may form within PHD finger protein 13 between cysteines 249 and 277.

Details

Redox score ?

90

PDB code

Structure name

phd-type zinc finger of human phd finger protein 13

Structure deposition date

2010-07-29

Thiol separation (Å)

4

Half-sphere exposure sum ?

42

Minimum pK_a ?

5

% buried

0

Peptide accession

Residue number A

249

Residue number B

277

Peptide name

PHD finger protein 13

Ligandability

Cysteine 249 of PHD finger protein 13

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 277 of PHD finger protein 13

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 PHD finger protein 13 between cysteines 249 and 252.

Details

Redox score ?

88

PDB code

Structure name

crystal structure of phf13 in complex with h3k4me3

Structure deposition date

2010-07-30

Thiol separation (Å)

4

Half-sphere exposure sum ?

49

Minimum pK_a ?

5

% buried

5

Peptide accession

Residue number A

249

Residue number B

252

Peptide name

PHD finger protein 13

Ligandability

Cysteine 249 of PHD finger protein 13

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 252 of PHD finger protein 13

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 PHD finger protein 13 between cysteines 249 and 274.

Details

Redox score ?

87

PDB code

Structure name

crystal structure of phf13 in complex with h3k4me3

Structure deposition date

2010-07-30

Thiol separation (Å)

4

Half-sphere exposure sum ?

59

Minimum pK_a ?

5

% buried

7

Peptide accession

Residue number A

249

Residue number B

274

Peptide name

PHD finger protein 13

Ligandability

Cysteine 249 of PHD finger protein 13

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 274 of PHD finger protein 13

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 PHD finger protein 13 between cysteines 252 and 277.

Details

Redox score ?

86

PDB code

Structure name

phd-type zinc finger of human phd finger protein 13

Structure deposition date

2010-07-29

Thiol separation (Å)

4

Half-sphere exposure sum ?

34

Minimum pK_a ?

7

% buried

0

Peptide accession

Residue number A

252

Residue number B

277

Peptide name

PHD finger protein 13

Ligandability

Cysteine 252 of PHD finger protein 13

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 277 of PHD finger protein 13

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 PHD finger protein 13 between cysteines 252 and 274.

Details

Redox score ?

85

PDB code

Structure name

phd-type zinc finger of human phd finger protein 13

Structure deposition date

2010-07-29

Thiol separation (Å)

4

Half-sphere exposure sum ?

45

Minimum pK_a ?

7

% buried

0

Peptide accession

Residue number A

252

Residue number B

274

Peptide name

PHD finger protein 13

Ligandability

Cysteine 252 of PHD finger protein 13

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 274 of PHD finger protein 13

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 PHD finger protein 13 between cysteines 235 and 237.

Details

Redox score ?

83

PDB code

Structure name

crystal structure of phf13 in complex with h3k4me3

Structure deposition date

2010-07-30

Thiol separation (Å)

4

Half-sphere exposure sum ?

48

Minimum pK_a ?

7

% buried

13

Peptide accession

Residue number A

235

Residue number B

237

Peptide name

PHD finger protein 13

Ligandability

Cysteine 235 of PHD finger protein 13

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 237 of PHD finger protein 13

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 PHD finger protein 13 between cysteines 274 and 277.

Details

Redox score ?

83

PDB code

Structure name

phd-type zinc finger of human phd finger protein 13

Structure deposition date

2010-07-29

Thiol separation (Å)

4

Half-sphere exposure sum ?

43

Minimum pK_a ?

9

% buried

0

Peptide accession

Residue number A

274

Residue number B

277

Peptide name

PHD finger protein 13

Ligandability

Cysteine 274 of PHD finger protein 13

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 277 of PHD finger protein 13

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 PHD finger protein 13 between cysteines 237 and 260.

Details

Redox score ?

81

PDB code

Structure name

phd-type zinc finger of human phd finger protein 13

Structure deposition date

2010-07-29

Thiol separation (Å)

4

Half-sphere exposure sum ?

40

Minimum pK_a ?

8

% buried

2

Peptide accession

Residue number A

237

Residue number B

260

Peptide name

PHD finger protein 13

Ligandability

Cysteine 237 of PHD finger protein 13

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 260 of PHD finger protein 13

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 PHD finger protein 13 between cysteines 235 and 260.

Details

Redox score ?

79

PDB code

Structure name

crystal structure of phf13 in complex with h3k4me3

Structure deposition date

2010-07-30

Thiol separation (Å)

4

Half-sphere exposure sum ?

53

Minimum pK_a ?

8

% buried

18

Peptide accession

Residue number A

235

Residue number B

260

Peptide name

PHD finger protein 13

Ligandability

Cysteine 235 of PHD finger protein 13

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 260 of PHD finger protein 13

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 PHD finger protein 13 between cysteines 235 and 274. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

52

PDB code

Structure name

crystal structure of phf13 in complex with h3k4me3

Structure deposition date

2010-07-30

Thiol separation (Å)

9

Half-sphere exposure sum ?

60

Minimum pK_a ?

8

% buried

16

Peptide accession

Residue number A

235

Residue number B

274

Peptide name

PHD finger protein 13

Ligandability

Cysteine 235 of PHD finger protein 13

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 274 of PHD finger protein 13

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 PHD finger protein 13 between cysteines 235 and 252. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

47

PDB code

Structure name

crystal structure of phf13 in complex with h3k4me3

Structure deposition date

2010-07-30

Thiol separation (Å)

10

Half-sphere exposure sum ?

50

Minimum pK_a ?

7

% buried

14

Peptide accession

Residue number A

235

Residue number B

252

Peptide name

PHD finger protein 13

Ligandability

Cysteine 235 of PHD finger protein 13

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 252 of PHD finger protein 13

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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