a tool for identifying drug-targetable redox-active disulphides

Protein CIP2A

Intramolecular

Cysteine 55 and cysteine 58

Cysteine 108 and cysteine 120 L

Cysteine 6 and cysteine 55

Cysteine 413 and cysteine 472 L

Cysteine 427 and cysteine 445

A redox-regulated disulphide may form within Protein CIP2A between cysteines 55 and 58.

Details

Redox score ?

64

PDB code

Structure name

crystal structure of a cip2a core domain

Structure deposition date

2017-01-04

Thiol separation (Å)

6

Half-sphere exposure sum ?

54

Minimum pK_a ?

10

% buried

24

Peptide accession

Residue number A

55

Residue number B

58

Peptide name

Protein CIP2A

Ligandability

Cysteine 55 of Protein CIP2A

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 58 of Protein CIP2A

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 Protein CIP2A between cysteines 108 and 120. 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 a cip2a core domain

Structure deposition date

2017-01-04

Thiol separation (Å)

9

Half-sphere exposure sum ?

nan

Minimum pK_a ?

10

% buried

44

Peptide accession

Residue number A

108

Residue number B

120

Peptide name

Protein CIP2A

Ligandability

Cysteine 108 of Protein CIP2A

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 120 of Protein CIP2A

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 Protein CIP2A between cysteines 6 and 55. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

46

PDB code

Structure name

crystal structure of a cip2a core domain

Structure deposition date

2017-01-04

Thiol separation (Å)

9

Half-sphere exposure sum ?

51

Minimum pK_a ?

9

% buried

14

Peptide accession

Residue number A

6

Residue number B

55

Peptide name

Protein CIP2A

Ligandability

Cysteine 6 of Protein CIP2A

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 55 of Protein CIP2A

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 Protein CIP2A between cysteines 413 and 472. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

38

PDB code

Structure name

crystal structure of a cip2a core domain

Structure deposition date

2017-01-04

Thiol separation (Å)

10

Half-sphere exposure sum ?

74

Minimum pK_a ?

9

% buried

63

Peptide accession

Residue number A

413

Residue number B

472

Peptide name

Protein CIP2A

Ligandability

Cysteine 413 of Protein CIP2A

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 472 of Protein CIP2A

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 Protein CIP2A between cysteines 427 and 445. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

33

PDB code

Structure name

crystal structure of a cip2a core domain

Structure deposition date

2017-01-04

Thiol separation (Å)

10

Half-sphere exposure sum ?

66

Minimum pK_a ?

11

% buried

80

Peptide accession

Residue number A

427

Residue number B

445

Peptide name

Protein CIP2A

Ligandability

Cysteine 427 of Protein CIP2A

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 445 of Protein CIP2A

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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