a tool for identifying drug-targetable redox-active disulphides

Haptoglobin

Intermolecular

Cysteine 33 and cysteine 33

Intramolecular

Cysteine 52 and cysteine 145

Cysteine 309 and cysteine 340

Cysteine 149 and cysteine 266

Cysteine 351 and cysteine 381

A redox-regulated disulphide may form between two units of Haptoglobin at cysteines 33 and 33.

Details

Redox score ?

94

PDB code

Structure name

structure of the haptoglobin-haemoglobin complex

Structure deposition date

2012-05-11

Thiol separation (Å)

2

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Haptoglobin

Peptide B name

Haptoglobin

Peptide A accession

Peptide B accession

Peptide A residue number

33

Peptide B residue number

33

Ligandability

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 Haptoglobin between cysteines 52 and 145 (111 and 145 respectively in this structure).

Details

Redox score ?

87

PDB code

Structure name

structure of t

Structure deposition date

2014-09-30

Thiol separation (Å)

2

Half-sphere exposure sum ?

53

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

52

Residue number B

145

Peptide name

Haptoglobin

Ligandability

Cysteine 52 of Haptoglobin

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 145 of Haptoglobin

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 Haptoglobin between cysteines 309 and 340 (305 and 336 respectively in this structure).

Details

Redox score ?

81

PDB code

Structure name

structure of t

Structure deposition date

2014-09-30

Thiol separation (Å)

2

Half-sphere exposure sum ?

79

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

309

Residue number B

340

Peptide name

Haptoglobin

Ligandability

Cysteine 309 of Haptoglobin

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 340 of Haptoglobin

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 Haptoglobin between cysteines 149 and 266 (149 and 262 respectively in this structure).

Details

Redox score ?

80

PDB code

Structure name

structure of t

Structure deposition date

2014-09-30

Thiol separation (Å)

2

Half-sphere exposure sum ?

72

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

149

Residue number B

266

Peptide name

Haptoglobin

Ligandability

Cysteine 149 of Haptoglobin

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 266 of Haptoglobin

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 Haptoglobin between cysteines 351 and 381.

Details

Redox score ?

78

PDB code

Structure name

human haptoglobin-haemoglobin complex

Structure deposition date

2014-11-21

Thiol separation (Å)

2

Half-sphere exposure sum ?

91

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

351

Residue number B

381

Peptide name

Haptoglobin

Ligandability

Cysteine 351 of Haptoglobin

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 381 of Haptoglobin

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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