a tool for identifying drug-targetable redox-active disulphides

Cyclin-H

Intramolecular

Cysteine 68 and cysteine 113

Cysteine 68 and cysteine 84

Cysteine 68 and cysteine 108

Cysteine 84 and cysteine 108

A redox-regulated disulphide may form within Cyclin-H between cysteines 68 and 113. 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

cyclin h, a positive regulatory subunit of cdk activating kinase

Structure deposition date

1996-08-08

Thiol separation (Å)

7

Half-sphere exposure sum ?

69

Minimum pK_a ?

12

% buried

77

Peptide accession

Residue number A

68

Residue number B

113

Peptide name

Cyclin-H

Ligandability

Cysteine 68 of Cyclin-H

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 113 of Cyclin-H

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 Cyclin-H between cysteines 68 and 84. 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

structure of cyclin mcs2

Structure deposition date

1996-10-11

Thiol separation (Å)

6

Half-sphere exposure sum ?

82

Minimum pK_a ?

12

% buried

96

Peptide accession

Residue number A

68

Residue number B

84

Peptide name

Cyclin-H

Ligandability

Cysteine 68 of Cyclin-H

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 84 of Cyclin-H

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 Cyclin-H between cysteines 68 and 108. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

27

PDB code

Structure name

structure of cyclin mcs2

Structure deposition date

1996-10-11

Thiol separation (Å)

10

Half-sphere exposure sum ?

80

Minimum pK_a ?

12

% buried

96

Peptide accession

Residue number A

68

Residue number B

108

Peptide name

Cyclin-H

Ligandability

Cysteine 68 of Cyclin-H

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 108 of Cyclin-H

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 Cyclin-H between cysteines 84 and 108. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

25

PDB code

Structure name

cyclin h, a positive regulatory subunit of cdk activating kinase

Structure deposition date

1996-08-08

Thiol separation (Å)

9

Half-sphere exposure sum ?

95

Minimum pK_a ?

13

% buried

100

Peptide accession

Residue number A

84

Residue number B

108

Peptide name

Cyclin-H

Ligandability

Cysteine 84 of Cyclin-H

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 108 of Cyclin-H

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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