a tool for identifying drug-targetable redox-active disulphides

C-X-C motif chemokine

Intramolecular

Cysteine 63 and cysteine 89

Cysteine 65 and cysteine 105

Cysteine 65 and cysteine 89

Cysteine 63 and cysteine 65

A redox-regulated disulphide may form within C-X-C motif chemokine between cysteines 63 and 89 (5 and 31 respectively in this structure).

Details

Redox score ?

83

PDB code

Structure name

ly3041658 fab bound to cxcl7

Structure deposition date

2020-05-14

Thiol separation (Å)

2

Half-sphere exposure sum ?

69

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

63

Residue number B

89

Peptide name

C-X-C motif chemokine

Ligandability

Cysteine 63 of C-X-C motif chemokine

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 89 of C-X-C motif chemokine

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 C-X-C motif chemokine between cysteines 65 and 105 (7 and 47 respectively in this structure).

Details

Redox score ?

80

PDB code

Structure name

ly3041658 fab bound to cxcl7

Structure deposition date

2020-05-14

Thiol separation (Å)

2

Half-sphere exposure sum ?

76

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

65

Residue number B

105

Peptide name

C-X-C motif chemokine

Ligandability

Cysteine 65 of C-X-C motif chemokine

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 105 of C-X-C motif chemokine

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 C-X-C motif chemokine between cysteines 65 and 89 (7 and 31 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

45

PDB code

Structure name

ly3041658 fab bound to cxcl7

Structure deposition date

2020-05-14

Thiol separation (Å)

8

Half-sphere exposure sum ?

73

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

65

Residue number B

89

Peptide name

C-X-C motif chemokine

Ligandability

Cysteine 65 of C-X-C motif chemokine

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 89 of C-X-C motif chemokine

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 C-X-C motif chemokine between cysteines 63 and 65 (5 and 7 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

42

PDB code

Structure name

ly3041658 fab bound to cxcl7

Structure deposition date

2020-05-14

Thiol separation (Å)

9

Half-sphere exposure sum ?

81

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

63

Residue number B

65

Peptide name

C-X-C motif chemokine

Ligandability

Cysteine 63 of C-X-C motif chemokine

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 65 of C-X-C motif chemokine

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.

If this tool was useful for finding a disulphide, please cite: