a tool for identifying drug-targetable redox-active disulphides

Beta-chimaerin

Intramolecular

Cysteine 245 and cysteine 248

Cysteine 245 and cysteine 264

Cysteine 248 and cysteine 264

Cysteine 228 and cysteine 256

Cysteine 231 and cysteine 256

Cysteine 228 and cysteine 231

Cysteine 276 and cysteine 277

A redox-regulated disulphide may form within Beta-chimaerin between cysteines 245 and 248 (243 and 246 respectively in this structure).

Details

Redox score ?

80

PDB code

Structure name

crystal structure of the human beta2-chimaerin

Structure deposition date

2004-08-25

Thiol separation (Å)

4

Half-sphere exposure sum ?

56

Minimum pK_a ?

7

% buried

40

Peptide accession

Residue number A

245

Residue number B

248

Peptide name

Beta-chimaerin

Ligandability

Cysteine 245 of Beta-chimaerin

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 248 of Beta-chimaerin

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 Beta-chimaerin between cysteines 245 and 264 (243 and 262 respectively in this structure).

Details

Redox score ?

77

PDB code

Structure name

crystal structure of the human beta2-chimaerin

Structure deposition date

2004-08-25

Thiol separation (Å)

5

Half-sphere exposure sum ?

54

Minimum pK_a ?

7

% buried

22

Peptide accession

Residue number A

245

Residue number B

264

Peptide name

Beta-chimaerin

Ligandability

Cysteine 245 of Beta-chimaerin

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 264 of Beta-chimaerin

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 Beta-chimaerin between cysteines 248 and 264 (246 and 262 respectively in this structure).

Details

Redox score ?

74

PDB code

Structure name

crystal structure of the human beta2-chimaerin

Structure deposition date

2004-08-25

Thiol separation (Å)

4

Half-sphere exposure sum ?

54

Minimum pK_a ?

9

% buried

34

Peptide accession

Residue number A

248

Residue number B

264

Peptide name

Beta-chimaerin

Ligandability

Cysteine 248 of Beta-chimaerin

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 264 of Beta-chimaerin

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 Beta-chimaerin between cysteines 228 and 256 (226 and 254 respectively in this structure).

Details

Redox score ?

72

PDB code

Structure name

crystal structure of the human beta2-chimaerin

Structure deposition date

2004-08-25

Thiol separation (Å)

4

Half-sphere exposure sum ?

71

Minimum pK_a ?

10

% buried

nan

Peptide accession

Residue number A

228

Residue number B

256

Peptide name

Beta-chimaerin

Ligandability

Cysteine 228 of Beta-chimaerin

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 Beta-chimaerin

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 Beta-chimaerin between cysteines 231 and 256 (229 and 254 respectively in this structure).

Details

Redox score ?

65

PDB code

Structure name

crystal structure of the human beta2-chimaerin

Structure deposition date

2004-08-25

Thiol separation (Å)

4

Half-sphere exposure sum ?

68

Minimum pK_a ?

10

% buried

74

Peptide accession

Residue number A

231

Residue number B

256

Peptide name

Beta-chimaerin

Ligandability

Cysteine 231 of Beta-chimaerin

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 Beta-chimaerin

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 Beta-chimaerin between cysteines 228 and 231 (226 and 229 respectively in this structure). 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 the human beta2-chimaerin

Structure deposition date

2004-08-25

Thiol separation (Å)

4

Half-sphere exposure sum ?

75

Minimum pK_a ?

19

% buried

nan

Peptide accession

Residue number A

228

Residue number B

231

Peptide name

Beta-chimaerin

Ligandability

Cysteine 228 of Beta-chimaerin

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 231 of Beta-chimaerin

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 Beta-chimaerin between cysteines 276 and 277 (274 and 275 respectively in this structure). 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 the human beta2-chimaerin

Structure deposition date

2004-08-25

Thiol separation (Å)

8

Half-sphere exposure sum ?

71

Minimum pK_a ?

12

% buried

100

Peptide accession

Residue number A

276

Residue number B

277

Peptide name

Beta-chimaerin

Ligandability

Cysteine 276 of Beta-chimaerin

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 Beta-chimaerin

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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