a tool for identifying drug-targetable redox-active disulphides

H2-M beta 2

Intramolecular

Cysteine 29 and cysteine 97

Cysteine 135 and cysteine 192

Cysteine 43 and cysteine 53

Cysteine 53 and cysteine 64

Cysteine 43 and cysteine 64

A redox-regulated disulphide may form within H2-M beta 2 between cysteines 29 and 97 (10 and 78 respectively in this structure).

Details

Redox score ?

81

PDB code

Structure name

crystal structure of mouse h2-dm

Structure deposition date

2001-10-24

Thiol separation (Å)

2

Half-sphere exposure sum ?

69

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

29

Residue number B

97

Peptide name

H2-M beta 2

Ligandability

Cysteine 29 of H2-M beta 2

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 97 of H2-M beta 2

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 H2-M beta 2 between cysteines 135 and 192 (116 and 173 respectively in this structure).

Details

Redox score ?

80

PDB code

Structure name

crystal structure of mouse h2-dm

Structure deposition date

2001-10-24

Thiol separation (Å)

2

Half-sphere exposure sum ?

79

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

135

Residue number B

192

Peptide name

H2-M beta 2

Ligandability

Cysteine 135 of H2-M beta 2

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 192 of H2-M beta 2

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 H2-M beta 2 between cysteines 43 and 53 (24 and 34 respectively in this structure).

Details

Redox score ?

79

PDB code

Structure name

crystal structure of mouse h2-dm

Structure deposition date

2001-10-24

Thiol separation (Å)

2

Half-sphere exposure sum ?

74

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

43

Residue number B

53

Peptide name

H2-M beta 2

Ligandability

Cysteine 43 of H2-M beta 2

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 53 of H2-M beta 2

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 H2-M beta 2 between cysteines 53 and 64 (34 and 45 respectively in this structure).

Details

Redox score ?

66

PDB code

Structure name

crystal structure of mouse h2-dm

Structure deposition date

2001-10-24

Thiol separation (Å)

4

Half-sphere exposure sum ?

62

Minimum pK_a ?

10

% buried

nan

Peptide accession

Residue number A

53

Residue number B

64

Peptide name

H2-M beta 2

Ligandability

Cysteine 53 of H2-M beta 2

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 64 of H2-M beta 2

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 H2-M beta 2 between cysteines 43 and 64 (24 and 45 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

55

PDB code

Structure name

crystal structure of mouse h2-dm

Structure deposition date

2001-10-24

Thiol separation (Å)

6

Half-sphere exposure sum ?

66

Minimum pK_a ?

10

% buried

nan

Peptide accession

Residue number A

43

Residue number B

64

Peptide name

H2-M beta 2

Ligandability

Cysteine 43 of H2-M beta 2

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 64 of H2-M beta 2

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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